Escherichia coli K-12 substr. MG1655 Polypeptide: maltose ABC transporter - periplasmic binding protein

Gene: malE Accession Numbers: EG10554 (EcoCyc), b4034, ECK4026

Synonyms: MBP, maltodextrin binding protein, maltose binding protein

Regulation Summary Diagram: ?

Regulation summary diagram for malE

Component of: maltose ABC transporter (extended summary available)

malE encodes the periplasmic substrate-binding component of the maltose ABC transporter. MalE, or maltodextrin binding protein (MBP) can bind linear maltodextrins from 2 - 7 glucose units in length but cannot bind the glucose monomer. MBP can also bind cyclic maltodextrins [Kellermann74, Miller83c, Spurlino91]. MBP is essential for the transport of maltose although mutants have been isolated which are able to transport maltose independently of MBP [Shuman82]

MBP consists of two globular domains separated by a deep groove which contains the maltodextrin binding site. MBP adopts two distinct conformations - an open unliganded form in which the two globular domains are far apart and the binding groove is accessible and a closed liganded structure. Bound maltose is almost completely enclosed and is held in place by hydrogen bonds and Van der Waals interactions [Spurlino91, Sharff92].

Maltose bound MBP has a strong stimulatory effect on the ATPase activity of the maltose transporter (MalFGK2) in vitro [Davidson92, Orelle08]. Both liganded and unliganded forms of MBP interact with the membrane components of the maltose transporter in vitro [Merino95, Bohl95] and unliganded MBP is also able to stimulate the ATPase activity of MalFGK2 [Gould09]. The interaction of both liganded and unliganded MalE with MalFGK2 in different nucleotide states (apo, ADP and ATP) has been investigated [Bohm13]. Dissociation of MBP is not a prerequisite for substrate translocation [Bohm13].

MBP is expressed at very high levels in the periplasm of E. coli growing on maltose [Kellermann74, Dietzel78].

In addition to being the periplasmic substrate-binding component of the maltose ABC transporter, MalE with bound substrate is also able to bind to the chemoreceptor Tar to induce chemotaxis toward maltose. MalE mutants have been identified which are chemotaxis negative for maltose [Hazelbauer75, Zhang92c, Zhang99].

Export of proMalE to the periplasm is dependent on the cytoplasmic chaperone SecB and this process has been extensively studied (reviewed by [Bassford90]

Reviews: [Martineau, Shilton08]

Citations: [Caldelari08, Quiocho79, Walters13, Austermuhle04, Ferenci86, Treptow85, Collier89, Weiss90, Collier88, Gannon89, Strobel93, Rosemond94, Hor93, Treptow88, Bucher11, Hall97, Hall97a, Hall97b, Gardina97, Kossmann88]

Gene Citations: [Francoz88]

Locations: inner membrane, periplasmic space

Map Position: [4,243,252 <- 4,244,442] (91.46 centisomes, 329°)
Length: 1191 bp / 396 aa

Molecular Weight of Polypeptide: 43.388 kD (from nucleotide sequence), 44.0 kD (experimental) [Kellermann74 ]

Unification Links: ASAP:ABE-0013200 , CGSC:532 , DIP:DIP-31871N , EchoBASE:EB0549 , EcoGene:EG10554 , EcoliWiki:b4034 , ModBase:P0AEX9 , OU-Microarray:b4034 , PortEco:malE , PR:PRO_000023147 , Pride:P0AEX9 , Protein Model Portal:P0AEX9 , RefSeq:NP_418458 , RegulonDB:EG10554 , SMR:P0AEX9 , String:511145.b4034 , Swiss-Model:P0AEX9 , UniProt:P0AEX9

Relationship Links: InterPro:IN-FAMILY:IPR006059 , InterPro:IN-FAMILY:IPR006060 , InterPro:IN-FAMILY:IPR006061 , PDB:Structure:1A7L , PDB:Structure:1ANF , PDB:Structure:1DMB , PDB:Structure:1ez9 , PDB:Structure:1ezo , PDB:Structure:1ezp , PDB:Structure:1fqa , PDB:Structure:1fqb , PDB:Structure:1fqc , PDB:Structure:1fqd , PDB:Structure:1HSJ , PDB:Structure:1IUD , PDB:Structure:1jvx , PDB:Structure:1JVY , PDB:Structure:1JW4 , PDB:Structure:1JW5 , PDB:Structure:1lax , PDB:Structure:1LLS , PDB:Structure:1MDP , PDB:Structure:1MDQ , PDB:Structure:1MG1 , PDB:Structure:1MH3 , PDB:Structure:1MH4 , PDB:Structure:1MPB , PDB:Structure:1MPC , PDB:Structure:1MPD , PDB:Structure:1n3w , PDB:Structure:1n3x , PDB:Structure:1nl5 , PDB:Structure:1NMU , PDB:Structure:1OMP , PDB:Structure:1peb , PDB:Structure:1R6Z , PDB:Structure:1svx , PDB:Structure:1T0K , PDB:Structure:1Y4C , PDB:Structure:1YTV , PDB:Structure:1ziu , PDB:Structure:1zjl , PDB:Structure:1ZKB , PDB:Structure:1zmg , PDB:Structure:2d21 , PDB:Structure:2h25 , PDB:Structure:2KLF , PDB:Structure:2NVU , PDB:Structure:2OBG , PDB:Structure:2OK2 , PDB:Structure:2r6g , PDB:Structure:2v93 , PDB:Structure:2VGQ , PDB:Structure:2XZ3 , PDB:Structure:2ZXT , PDB:Structure:3A3C , PDB:Structure:3C4M , PDB:Structure:3CSB , PDB:Structure:3CSG , PDB:Structure:3DM0 , PDB:Structure:3EHS , PDB:Structure:3EHT , PDB:Structure:3EHU , PDB:Structure:3F5F , PDB:Structure:3G7V , PDB:Structure:3G7W , PDB:Structure:3H3G , PDB:Structure:3H4Z , PDB:Structure:3HPI , PDB:Structure:3HST , PDB:Structure:3IO4 , PDB:Structure:3IO6 , PDB:Structure:3IOR , PDB:Structure:3IOT , PDB:Structure:3IOU , PDB:Structure:3IOV , PDB:Structure:3IOW , PDB:Structure:3KJT , PDB:Structure:3L2J , PDB:Structure:3LBS , PDB:Structure:3LC8 , PDB:Structure:3MBP , PDB:Structure:3MP1 , PDB:Structure:3MP6 , PDB:Structure:3MP8 , PDB:Structure:3MQ9 , PDB:Structure:3N94 , PDB:Structure:3O3U , PDB:Structure:3OAI , PDB:Structure:3OSQ , PDB:Structure:3OSR , PDB:Structure:3PGF , PDB:Structure:3PUV , PDB:Structure:3PUW , PDB:Structure:3PUX , PDB:Structure:3PUY , PDB:Structure:3PUZ , PDB:Structure:3PV0 , PDB:Structure:3PY7 , PDB:Structure:3Q25 , PDB:Structure:3Q26 , PDB:Structure:3Q27 , PDB:Structure:3Q28 , PDB:Structure:3Q29 , PDB:Structure:3RLF , PDB:Structure:3RUM , PDB:Structure:3SER , PDB:Structure:3SES , PDB:Structure:3SET , PDB:Structure:3SEU , PDB:Structure:3SEV , PDB:Structure:3SEW , PDB:Structure:3SEX , PDB:Structure:3SEY , PDB:Structure:3VFJ , PDB:Structure:3W15 , PDB:Structure:3WAI , PDB:Structure:4B3N , PDB:Structure:4BL8 , PDB:Structure:4BL9 , PDB:Structure:4BLA , PDB:Structure:4BLB , PDB:Structure:4BLD , PDB:Structure:4DXB , PDB:Structure:4DXC , PDB:Structure:4EDQ , PDB:Structure:4EGC , PDB:Structure:4EXK , PDB:Structure:4FE8 , PDB:Structure:4FEB , PDB:Structure:4FEC , PDB:Structure:4FED , PDB:Structure:4GIZ , PDB:Structure:4GLI , PDB:Structure:4IFP , PDB:Structure:4IKM , PDB:Structure:4IRL , PDB:Structure:4JBZ , PDB:Structure:4JKM , PDB:Structure:4KEG , PDB:Structure:4KHZ , PDB:Structure:4KI0 , PDB:Structure:4KV3 , PDB:Structure:4KYC , PDB:Structure:4KYD , PDB:Structure:4KYE , PDB:Structure:4MBP , PDB:Structure:4N4X , PDB:Structure:4NDZ , PDB:Structure:4R0Y ... [3 more not displayed]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for malE

GO Terms:

Biological Process: GO:0006810 - transport Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Davidson90]
GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0008643 - carbohydrate transport Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Davidson90]
GO:0015768 - maltose transport Inferred from experiment Inferred by computational analysis [GOA01a, Ferenci80, Davidson90, Shuman82, Davidson91]
GO:0034289 - detection of maltose stimulus Inferred from experiment [Hazelbauer75, Zhang92c]
GO:0042956 - maltodextrin transport Inferred from experiment [Ferenci80]
GO:0060326 - cell chemotaxis Inferred from experiment [Hazelbauer75, Zhang92c]
Molecular Function: GO:0005215 - transporter activity Inferred from experiment Inferred by computational analysis [GOA01a, Davidson90]
GO:0005515 - protein binding Inferred from experiment [Oldham11, Daus09, Sharma08]
GO:1901982 - maltose binding Inferred from experiment [Kellermann74]
GO:0005363 - maltose transmembrane transporter activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred from experiment Inferred by computational analysis [DiazMejia09, Han14, LopezCampistrou05, Kellermann74]
GO:0042597 - periplasmic space Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Spurlino91]
GO:0043190 - ATP-binding cassette (ABC) transporter complex Inferred from experiment [Davidson90]
GO:0055052 - ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing Inferred from experiment [Davidson90]
GO:1990060 - maltose transport complex Inferred from experiment [Davidson90]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases ABC superfamily, periplasmic binding component

Essentiality data for malE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of: maltose ABC transporter

Subunit composition of maltose ABC transporter = [MalK]2[MalF][MalG][MalE]
         maltose ABC transporter - ATP binding subunit = MalK (summary available)
         maltose ABC transporter - membrane subunit = MalF (summary available)
         maltose ABC transporter - membrane subunit = MalG (summary available)
         maltose ABC transporter - periplasmic binding protein = MalE (extended summary available)

MalKFGE is a maltose transport system that is a member of the ATP-Binding Cassette (ABC) Superfamily of transporters [Wu95]. MalE is the periplasmic maltose-binding protein, MalF and MalG are the integral membrane components, and MalK is the ATP-binding component of the ABC transporter, peripherally associated with the inner membrane through its interactions with MalF and MalG. The maltose ABC transporter is capable of transporting malto-oligosaccharides up to seven glucose units long [Ferenci80]. The maltose transporter also functions to regulate gene expression through direct interaction with its cognate transcriptional regulator MalT [Richet12].

The crystal structure of the maltose ABC transporter has been determined in 3 differing conformations: an inward facing 'resting' state with the maltose binding pocket only accessible from the cytoplasm and the nucleotide binding interface in an open conformation [Khare09]; an outward facing conformation with the substrate binding pocket open towards the periplasmic space and ATP bound at the cytoplasmic nucleotide binding interface [Oldham07] and an intermediate 'pre-translocation' structure with an occluded maltose binding pocket and no ATP bound [Oldham11].

The structure of MalE has been studied extensively [Sharff92, Spurlino91, Sharff95, Sharff93, Shilton96, Quiocho97, Mueller00, Duan01, Duan02, Rubin02, Srinivasan02, Saul03, Telmer03, Binz04, Telmer05, Kainosho06, Xu06a, Tang07]. The crystal structure of the dimeric MalK has also been determined with bound ADP to a resolution of 2.3 Å [Lu05a], with ATP bound to 2.60 Å, in a nucleotide-free, open state to 2.8 Å, and in a nucleotide-free semi-open state to 2.9 Å [Chen03a]. The N-terminal portion of MalK is the ATP-binding portion which interacts with MalF and MalG, and the C-terminal portion is a regulatory domain that interacts with MalT to prevent transcription of mal genes [Higgins85, Bohm02, Samanta03, Chen03a]. Binding of ATP to MalK is required for stabilization of the MalEFGK2 complex [Chen01b]. Binding of ATP to MalK results in closure of the MalK dimer interface and transmission of a signal through MalF and MalG causing the opening of MalE to release maltose into the transporter [Mourez98, Mannering01, Austermuhle04, Daus06, Oloo06, Wen08]. Binding of MalE to the MalF and MalG subunits of MalFGK2 stimulates ATPase activity of the MalK subunits coupled to substrate transport [Chen01b, Daus07]. The signal for stimulation of ATPase activity is transduced through MalF and MalG [Davidson92, Covitz94]. The interaction of MalF,and in particular the large periplasmic loop of MalF, with MalE has been studied [Daus09, Jacso09].

A 10-fold increase in the level of maltose transport activity was observed in membrane vesicles when the membrane associated components of the transport system (MalF, MalG, and MalK) were overproduced [Davidson90]. Maltose transport activity was abolished in proteoliposomes prepared from a strain with a deletion of the mal genes [Davidson90]. The purified MalKFGE complex exhibits transport-associated ATPase activity, and mutations in the malK gene resulted in loss of ATPase and transport activities without affecting protein stability [Davidson91, Panagiotidis93, Davidson97]. malF mutants are able to transport lactose through the maltose ABC transporter [Merino97, Merino98].

Expression of the malE and malK operons is activated by MalT and cAMP-CRP [VidalIngigliard91, Chapon82, Hofnung74, Hofnung74a]. Inactive (ATP-bound) MalK inhibits the activation of MalT by competing with the binding of the inducer, maltotriose, to MalT [Joly04, Reyes88]. MalK with hydrolysed ATP no longer associates with and inhibits MalT [Panagiotidis98]. Inhibition involves sequestration of MalT by the resting form of the MalFGK transporter, not by free MalK. In the absence of maltose, MalT is sequestered by the maltose transporter via a MalK-MalT interaction; upon addition of maltose to the culture medium, MalT is released from the membrane [Richet12]. This mechanism prevents the induction of malT by endogenously produced maltotriose and directly couples transport with the activation of a transcriptional regulator.

MalY and Aes also inhibit activation of MalT by competing with maltotriose [Reidl91, Schreiber00, Clausen00, Joly02, Schlegel02]. Lrp activates expression of the malE and malK operons [Tchetina95]. Mlc acts as a repressor of malT expression [Decker98]. Transcription of malE is regulated by the CreBC two-component system [Avison01]. MalK activity is also subject to inducer exclusion, that is, direct allosteric inhibition, by the dephosphorylated form of EIIAGlc. Addition of EIIAGlc inhibits the activity of the maltose transporter reconstituted in proteopliposomes [Dean90, Bao13]. The pH-dependent transcription of the maltose regulon is dependent upon the level of cAMP-CRP [Chagneau01, Alonzo98].

Targeting of MalE to the Sec-translocase for transport across the inner membrane is SecB-dependent [Bechtluft07, Baars06]. Insertion of MalF into the cytoplasmic membrane is SecE- and SecA-dependent [Traxler96, Saaf95], though evidence to the contrary has been presented [McGovern91].

Reviews: [Schlegel02a, Boos98, Nikaido94, Shuman93, Bordignon10, Gorke12, Chen13a].

Citations: [Daus07a, Sharma05, Richet05, Kennedy04a, Steinke01, Sharma00, Hunke00, ReichSlotky00, Decker99, Kennedy99, Nelson98, Panagiotidis98a, Hall98, Mourez97, Mourez97a, Dassa97, Lippincott97, Meyer97, Richet96, Zhang96c, Ehrle96, Schneider95, Hekstra93, Boyd93, Dassa93, Dassa93a, Traxler92, Dean92, McGovern91a, Ehrmann91, Ehrmann90, Wyka90, Francoz88, Froshauer88, Newbury87, Boyd87, Ehrmann87, Duplay87, Bukau86, Froshauer84, Kiino84, Bedouelle83, Ohsumi83, Gilson82, Bedouelle82, Ohki82, Shuman82a, Bedouelle82a, Shuman81, Colonna81, Wandersman79, Raibaud79, Silhavy79, Raibaud79a, Randall78, Bao13a]

Locations: inner membrane

Relationship Links: PDB:Structure:2R6G , PDB:Structure:3FH6 , PDB:Structure:3PUY , PDB:Structure:3PUZ , PDB:Structure:3PV0

GO Terms:

Biological Process: GO:0015768 - maltose transport Inferred from experiment [Davidson91]
Molecular Function: GO:0015423 - maltose-transporting ATPase activity Inferred from experiment [Davidson91]
GO:0015609 - maltooligosaccharide-importing ATPase activity Inferred from experiment [Ferenci80]
GO:0033613 - activating transcription factor binding Inferred from experiment [Richet12]
Cellular Component: GO:0043190 - ATP-binding cassette (ABC) transporter complex Inferred from experiment [Davidson91]

Enzymatic reaction of: maltotetraose ABC transporter (maltose ABC transporter)

EC Number: 3.6.3.-

Transport reaction diagram for maltotetraose ABC transporter

Enzymatic reaction of: maltotriose ABC transporter (maltose ABC transporter)

EC Number: 3.6.3.-

Transport reaction diagram for maltotriose ABC transporter

Enzymatic reaction of: maltose ABC transporter

Synonyms: Transport of maltose

EC Number:

Transport reaction diagram for maltose ABC transporter

Alternative Products for maltose: maltohexaose [Ferenci80 ] , maltopentaose [Ferenci80 ] , maltoheptaose [Ferenci80 ]

Sequence Features

Protein sequence of maltose ABC transporter - periplasmic binding protein with features indicated

Feature Class Location Common Name Citations Comment
Signal-Sequence 1 -> 26 MalE signal sequence
[Wilkins98, Link97, Bedouelle80]
Chain 27 -> 396  
UniProt: Maltose-binding periplasmic protein;
Sequence-Conflict 36  
[Link97, UniProt10]
UniProt: (in Ref. 8; AA sequence);
Sequence-Conflict 46  
[Bedouelle82a, UniProt10]
UniProt: (in Ref. 5);

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b4034 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10554.


Alonzo98: Alonzo S, Heyde M, Laloi P, Portalier R (1998). "Analysis of the effect exerted by extracellular pH on the maltose regulon in Escherichia coli K-12." Microbiology 144 ( Pt 12);3317-25. PMID: 9884223

Austermuhle04: Austermuhle MI, Hall JA, Klug CS, Davidson AL (2004). "Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport." J Biol Chem 279(27);28243-50. PMID: 15117946

Avison01: Avison MB, Horton RE, Walsh TR, Bennett PM (2001). "Escherichia coli CreBC is a global regulator of gene expression that responds to growth in minimal media." J Biol Chem 276(29);26955-61. PMID: 11350954

Baars06: Baars L, Ytterberg AJ, Drew D, Wagner S, Thilo C, van Wijk KJ, de Gier JW (2006). "Defining the role of the Escherichia coli chaperone SecB using comparative proteomics." J Biol Chem 281(15);10024-34. PMID: 16352602

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bao13: Bao H, Duong F (2013). "Phosphatidylglycerol directs binding and inhibitory action of EIIAGlc protein on the maltose transporter." J Biol Chem 288(33);23666-74. PMID: 23821551

Bao13a: Bao H, Duong F (2013). "ATP alone triggers the outward facing conformation of the maltose ATP-binding cassette transporter." J Biol Chem 288(5);3439-48. PMID: 23243313

Bassford90: Bassford PJ (1990). "Export of the periplasmic maltose-binding protein of Escherichia coli." J Bioenerg Biomembr 22(3);401-39. PMID: 2202725

Bechtluft07: Bechtluft P, van Leeuwen RG, Tyreman M, Tomkiewicz D, Nouwen N, Tepper HL, Driessen AJ, Tans SJ (2007). "Direct observation of chaperone-induced changes in a protein folding pathway." Science 318(5855);1458-61. PMID: 18048690

Bedouelle80: Bedouelle H, Bassford PJ, Fowler AV, Zabin I, Beckwith J, Hofnung M (1980). "Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli." Nature 285(5760);78-81. PMID: 6990274

Bedouelle82: Bedouelle H, Schmeissner U, Hofnung M, Rosenberg M (1982). "Promoters of the malEFG and malK-lamB operons in Escherichia coli K12." J Mol Biol 161(4);519-31. PMID: 6185687

Bedouelle82a: Bedouelle H, Hofnung M (1982). "A DNA sequence containing the control regions of the malEFG and malK-lamB operons in Escherichia coli K12." Mol Gen Genet 185(1);82-7. PMID: 6283312

Bedouelle83: Bedouelle H (1983). "Mutations in the promoter regions of the malEFG and malK-lamB operons of Escherichia coli K12." J Mol Biol 170(4);861-82. PMID: 6417341

Binz04: Binz HK, Amstutz P, Kohl A, Stumpp MT, Briand C, Forrer P, Grutter MG, Pluckthun A (2004). "High-affinity binders selected from designed ankyrin repeat protein libraries." Nat Biotechnol 22(5);575-82. PMID: 15097997

Bohl95: Bohl E, Shuman HA, Boos W (1995). "Mathematical treatment of the kinetics of binding protein dependent transport systems reveals that both the substrate loaded and unloaded binding proteins interact with the membrane components." J Theor Biol 172(1);83-94. PMID: 7891451

Bohm02: Bohm A, Diez J, Diederichs K, Welte W, Boos W (2002). "Structural model of MalK, the ABC subunit of the maltose transporter of Escherichia coli: implications for mal gene regulation, inducer exclusion, and subunit assembly." J Biol Chem 277(5);3708-17. PMID: 11709552

Bohm13: Bohm S, Licht A, Wuttge S, Schneider E, Bordignon E (2013). "Conformational plasticity of the type I maltose ABC importer." Proc Natl Acad Sci U S A 110(14);5492-7. PMID: 23509285

Boos98: Boos W, Shuman H (1998). "Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation." Microbiol Mol Biol Rev 62(1);204-29. PMID: 9529892

Bordignon10: Bordignon E, Grote M, Schneider E (2010). "The maltose ATP-binding cassette transporter in the 21st century--towards a structural dynamic perspective on its mode of action." Mol Microbiol 77(6);1354-66. PMID: 20659291

Boyd87: Boyd D, Manoil C, Beckwith J (1987). "Determinants of membrane protein topology." Proc Natl Acad Sci U S A 84(23);8525-9. PMID: 3317413

Boyd93: Boyd D, Traxler B, Beckwith J (1993). "Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions." J Bacteriol 175(2);553-6. PMID: 8419303

Bucher11: Bucher D, Grant BJ, Markwick PR, McCammon JA (2011). "Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamics." PLoS Comput Biol 7(4);e1002034. PMID: 21533070

Bukau86: Bukau B, Ehrmann M, Boos W (1986). "Osmoregulation of the maltose regulon in Escherichia coli." J Bacteriol 166(3);884-91. PMID: 2423504

Caldelari08: Caldelari I, Palmer T, Sargent F (2008). "Escherichia coli tat mutant strains are able to transport maltose in the absence of an active malE gene." Arch Microbiol 189(6);597-604. PMID: 18385983

Chagneau01: Chagneau C, Heyde M, Alonso S, Portalier R, Laloi P (2001). "External-pH-dependent expression of the maltose regulon and ompF gene in Escherichia coli is affected by the level of glycerol kinase, encoded by glpK." J Bacteriol 183(19);5675-83. PMID: 11544231

Chapon82: Chapon C (1982). "Role of the catabolite activator protein in the maltose regulon of Escherichia coli." J Bacteriol 150(2);722-9. PMID: 7040340

Chen01b: Chen J, Sharma S, Quiocho FA, Davidson AL (2001). "Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport." Proc Natl Acad Sci U S A 98(4);1525-30. PMID: 11171984

Chen03a: Chen J, Lu G, Lin J, Davidson AL, Quiocho FA (2003). "A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle." Mol Cell 12(3);651-61. PMID: 14527411

Chen13a: Chen J (2013). "Molecular mechanism of the Escherichia coli maltose transporter." Curr Opin Struct Biol. PMID: 23628288

Clausen00: Clausen T, Schlegel A, Peist R, Schneider E, Steegborn C, Chang YS, Haase A, Bourenkov GP, Bartunik HD, Boos W (2000). "X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression." EMBO J 19(5);831-42. PMID: 10698925

Collier88: Collier DN, Bankaitis VA, Weiss JB, Bassford PJ (1988). "The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein." Cell 53(2);273-83. PMID: 2834066

Collier89: Collier DN, Bassford PJ (1989). "Mutations that improve export of maltose-binding protein in SecB- cells of Escherichia coli." J Bacteriol 171(9);4640-7. PMID: 2670890

Colonna81: Colonna B, Hofnung M (1981). "rho Mutations restore lamB expression in E. coli K12 strains with an inactive malB region." Mol Gen Genet 184(3);479-83. PMID: 6278260

Covitz94: Covitz KM, Panagiotidis CH, Hor LI, Reyes M, Treptow NA, Shuman HA (1994). "Mutations that alter the transmembrane signalling pathway in an ATP binding cassette (ABC) transporter." EMBO J 13(7);1752-9. PMID: 8157012

Dassa93: Dassa E (1993). "Sequence-function relationships in MalG, an inner membrane protein from the maltose transport system in Escherichia coli." Mol Microbiol 7(1);39-47. PMID: 8437519

Dassa93a: Dassa E, Muir S (1993). "Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli." Mol Microbiol 7(1);29-38. PMID: 8437518

Dassa97: Dassa E, Lambert P (1997). "Activity of protein MalE (maltose-binding protein) fused to cytoplasmic and periplasmic regions of an Escherichia coli inner membrane protein." Res Microbiol 148(5);389-95. PMID: 9765817

Daus06: Daus ML, Landmesser H, Schlosser A, Muller P, Herrmann A, Schneider E (2006). "ATP induces conformational changes of periplasmic loop regions of the maltose ATP-binding cassette transporter." J Biol Chem 281(7);3856-65. PMID: 16352608

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Other References Related to Gene Regulation

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Merkel92: Merkel TJ, Nelson DM, Brauer CL, Kadner RJ (1992). "Promoter elements required for positive control of transcription of the Escherichia coli uhpT gene." J Bacteriol 1992;174(9);2763-70. PMID: 1569008

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Raibaud89a: Raibaud O (1989). "Nucleoprotein structures at positively regulated bacterial promoters: homology with replication origins and some hypotheses on the quaternary structure of the activator proteins in these complexes." Mol Microbiol 1989;3(3);455-8. PMID: 2664421

Richet00: Richet E (2000). "Synergistic transcription activation: a dual role for CRP in the activation of an Escherichia coli promoter depending on MalT and CRP." EMBO J 19(19);5222-32. PMID: 11013224

Richet91: Richet E, Raibaud O (1991). "Supercoiling is essential for the formation and stability of the initiation complex at the divergent malEp and malKp promoters." J Mol Biol 218(3);529-42. PMID: 2016744

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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