PDBsum entry 2dhh

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protein Protein-protein interface(s) links
Membrane protein PDB id
Jmol PyMol
Protein chains
1022 a.a. *
Waters ×56
* Residue conservation analysis
PDB id:
Name: Membrane protein
Title: Crystal structure of a multidrug transporter reveal a functionally rotating mechanism
Structure: Acrb. Chain: a, b, c. Synonym: multidrug efflux transporter, acriflavine resistance protein b. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli k12. Expression_system_taxid: 83333.
Biol. unit: Trimer (from PQS)
2.80Å     R-factor:   0.270     R-free:   0.307
Authors: S.Murakami,R.Nakashima,E.Yamashita,T.Matsumoto
Key ref:
S.Murakami et al. (2006). Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature, 443, 173-179. PubMed id: 16915237 DOI: 10.1038/nature05076
23-Mar-06     Release date:   22-Aug-06    
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Protein chains
Pfam   ArchSchema ?
P31224  (ACRB_ECOLI) -  Multidrug efflux pump subunit AcrB
1049 a.a.
1022 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   4 terms 
  Biological process     transport   4 terms 
  Biochemical function     transporter activity     5 terms  


DOI no: 10.1038/nature05076 Nature 443:173-179 (2006)
PubMed id: 16915237  
Crystal structures of a multidrug transporter reveal a functionally rotating mechanism.
S.Murakami, R.Nakashima, E.Yamashita, T.Matsumoto, A.Yamaguchi.
AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change.
  Selected figure(s)  
Figure 3.
Figure 3: The novel drug translocation pathway for AcrB.
Figure 3 : The novel drug translocation pathway for AcrB. Unfortunately we are unable to provide accessible alternative text for this. If you require assistance to access this image, or to obtain a text description, please contact
Bound minocycline in the binding protomer is shown in a CPK representation and coloured as in Fig. 1. a, Stereo-pair of the inner cavities inside the periplasmic region of AcrB viewed from the side parallel to the membrane plane as in Fig. 1a. The chicken-wire representation coloured in magenta is the solvent-accessible inner cavity of the AcrB molecule created with the program VOIDOO^42 and MAMA^43 of the Uppsala Software Factory ( with slight modifications (surface-noise removal, and so on). For clarity, the access protomer is removed. b, Close-up stereo views of the vestibules in three different transport states, viewed from slightly diagonally below to the side of the molecule. Three protomers are superposed using the least-squares superposition program LSQKAB, from the CCP4 program suite^33. The flexible region above TM8 and the PC2 subdomain are represented by solid colours corresponding to the colours in Fig. 1, and the remaining main-chain tracings are more transparent. The vestibule is indicated as a dotted circle.
Figure 4.
Figure 4: Structure with a slab ( approx-23 Å) of the transmembrane domain viewed from the periplasmic side. The side chains of three functionally essential charged residues—Asp 407, Asp 408 and Lys 940—and functionally important residue Thr 978 are shown in a ball-and-stick representation. Colours of the protomers are as in Fig. 1. Roman numerals indicate the transmembrane helix numbers^13.
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (2006, 443, 173-179) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20981744 C.C.Su, F.Long, and E.W.Yu (2011).
The Cus efflux system removes toxic ions via a methionine shuttle.
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21350490 C.C.Su, F.Long, M.T.Zimmermann, K.R.Rajashankar, R.L.Jernigan, and E.W.Yu (2011).
Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli.
  Nature, 470, 558-562.
PDB code: 3ne5
21112401 C.Ebel (2011).
Sedimentation velocity to characterize surfactants and solubilized membrane proteins.
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21513873 C.Oswald, and K.M.Pos (2011).
Drug resistance: a periplasmic ménage à trois.
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21148208 E.Nikaido, I.Shirosaka, A.Yamaguchi, and K.Nishino (2011).
Regulation of the AcrAB multidrug efflux pump in Salmonella enterica serovar Typhimurium in response to indole and paraquat.
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21286630 G.D.Wright (2011).
Molecular mechanisms of antibiotic resistance.
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21264225 K.M.Peters, B.E.Brooks, M.A.Schumacher, R.A.Skurray, R.G.Brennan, and M.H.Brown (2011).
A single acidic residue can guide binding site selection but does not govern QacR cationic-drug affinity.
  PLoS One, 6, e15974.
PDB code: 3pm1
21296164 N.Monroe, G.Sennhauser, M.A.Seeger, C.Briand, and M.G.Grütter (2011).
Designed ankyrin repeat protein binders for the crystallization of AcrB: Plasticity of the dominant interface.
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PDB codes: 3noc 3nog
21249122 R.Kulathila, R.Kulathila, M.Indic, and B.van den Berg (2011).
Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump.
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PDB code: 3pik
22121023 R.Nakashima, K.Sakurai, S.Yamasaki, K.Nishino, and A.Yamaguchi (2011).
Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket.
  Nature, 480, 565-569.
PDB codes: 3aoa 3aob 3aoc 3aod
21115481 T.K.Janganan, L.Zhang, V.N.Bavro, D.Matak-Vinkovic, N.P.Barrera, M.F.Burton, P.G.Steel, C.V.Robinson, M.I.Borges-Walmsley, and A.R.Walmsley (2011).
Opening of the outer membrane protein channel in tripartite efflux pumps is induced by interaction with the membrane fusion partner.
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21562494 T.Tsukazaki, H.Mori, Y.Echizen, R.Ishitani, S.Fukai, T.Tanaka, A.Perederina, D.G.Vassylyev, T.Kohno, A.D.Maturana, K.Ito, and O.Nureki (2011).
Structure and function of a membrane component SecDF that enhances protein export.
  Nature, 474, 235-238.
PDB codes: 2rrn 3aqo 3aqp
21245342 X.Y.Pei, P.Hinchliffe, M.F.Symmons, E.Koronakis, R.Benz, C.Hughes, and V.Koronakis (2011).
Structures of sequential open states in a symmetrical opening transition of the TolC exit duct.
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PDB codes: 2wmz 2xmn
19922410 A.Karasawa, K.Mitsui, M.Matsushita, and H.Kanazawa (2010).
Intermolecular cross-linking of monomers in Helicobacter pylori Na+/H+ antiporter NhaA at the dimer interface inhibits antiporter activity.
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20368395 A.Louie, C.Grasso, N.Bahniuk, B.Van Scoy, D.L.Brown, R.Kulawy, and G.L.Drusano (2010).
The combination of meropenem and levofloxacin is synergistic with respect to both Pseudomonas aeruginosa kill rate and resistance suppression.
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20583998 A.Welch, C.U.Awah, S.Jing, H.W.van Veen, and H.Venter (2010).
Promiscuous partnering and independent activity of MexB, the multidrug transporter protein from Pseudomonas aeruginosa.
  Biochem J, 430, 355-364.  
21221942 B.Y.Yun, Y.Xu, S.Piao, N.Kim, J.H.Yoon, H.S.Cho, K.Lee, and N.C.Ha (2010).
Periplasmic domain of CusA in an Escherichia coli Cu+/Ag+ transporter has metal binding sites.
  J Microbiol, 48, 829-835.  
20442961 E.H.Kim, C.Rensing, and M.M.McEvoy (2010).
Chaperone-mediated copper handling in the periplasm.
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20525265 E.Perrin, M.Fondi, M.C.Papaleo, I.Maida, S.Buroni, M.R.Pasca, G.Riccardi, and R.Fani (2010).
Exploring the HME and HAE1 efflux systems in the genus Burkholderia.
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20534468 F.De Angelis, J.K.Lee, J.D.O'Connell, L.J.Miercke, K.H.Verschueren, V.Srinivasan, C.Bauvois, C.Govaerts, R.A.Robbins, J.M.Ruysschaert, R.M.Stroud, and G.Vandenbussche (2010).
Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems.
  Proc Natl Acad Sci U S A, 107, 11038-11043.
PDB code: 3lnn
20804453 F.Husain, and H.Nikaido (2010).
Substrate path in the AcrB multidrug efflux pump of Escherichia coli.
  Mol Microbiol, 78, 320-330.  
20865003 F.Long, C.C.Su, M.T.Zimmermann, S.E.Boyken, K.R.Rajashankar, R.L.Jernigan, and E.W.Yu (2010).
Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport.
  Nature, 467, 484-488.
PDB codes: 3k07 3kso 3kss
20399187 G.Phan, H.Benabdelhak, M.B.Lascombe, P.Benas, S.Rety, M.Picard, A.Ducruix, C.Etchebest, and I.Broutin (2010).
Structural and dynamical insights into the opening mechanism of P. aeruginosa OprM channel.
  Structure, 18, 507-517.
PDB code: 3d5k
20038594 H.S.Kim, D.Nagore, and H.Nikaido (2010).
Multidrug efflux pump MdtBC of Escherichia coli is active only as a B2C heterotrimer.
  J Bacteriol, 192, 1377-1386.  
20962836 H.W.van Veen (2010).
Structural biology: Last of the multidrug transporters.
  Nature, 467, 926-927.  
20606071 J.A.Bohnert, B.Karamian, and H.Nikaido (2010).
Optimized Nile Red efflux assay of AcrAB-TolC multidrug efflux system shows competition between substrates.
  Antimicrob Agents Chemother, 54, 3770-3775.  
19940001 J.A.Lundbaek, S.A.Collingwood, H.I.Ingólfsson, R.Kapoor, and O.S.Andersen (2010).
Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes.
  J R Soc Interface, 7, 373-395.  
20132445 J.W.Weeks, T.Celaya-Kolb, S.Pecora, and R.Misra (2010).
AcrA suppressor alterations reverse the drug hypersensitivity phenotype of a TolC mutant by inducing TolC aperture opening.
  Mol Microbiol, 75, 1468-1483.  
19826804 K.McLuskey, A.W.Roszak, Y.Zhu, and N.W.Isaacs (2010).
Crystal structures of all-alpha type membrane proteins.
  Eur Biophys J, 39, 723-755.  
20667175 K.R.Vinothkumar, and R.Henderson (2010).
Structures of membrane proteins.
  Q Rev Biophys, 43, 65.  
19884363 N.Kamal, and W.M.Shafer (2010).
Biologic activities of the TolC-like protein of Neisseria meningitidis as assessed by functional complementation in Escherichia coli.
  Antimicrob Agents Chemother, 54, 506-508.  
20548943 R.Schulz, A.V.Vargiu, F.Collu, U.Kleinekathöfer, and P.Ruggerone (2010).
Functional rotation of the transporter AcrB: insights into drug extrusion from simulations.
  PLoS Comput Biol, 6, e1000806.  
20160052 S.P.Lim, and H.Nikaido (2010).
Kinetic parameters of efflux of penicillins by the multidrug efflux transporter AcrAB-TolC of Escherichia coli.
  Antimicrob Agents Chemother, 54, 1800-1806.  
20495209 T.Horiyama, A.Yamaguchi, and K.Nishino (2010).
TolC dependency of multidrug efflux systems in Salmonella enterica serovar Typhimurium.
  J Antimicrob Chemother, 65, 1372-1376.  
  20452953 T.J.Silhavy, D.Kahne, and S.Walker (2010).
The bacterial cell envelope.
  Cold Spring Harb Perspect Biol, 2, a000414.  
  21081915 X.Q.Yao, H.Kenzaki, S.Murakami, and S.Takada (2010).
Drug export and allosteric coupling in a multidrug transporter revealed by molecular simulations.
  Nat Commun, 1, 117.  
20212112 Y.Takatsuka, C.Chen, and H.Nikaido (2010).
Mechanism of recognition of compounds of diverse structures by the multidrug efflux pump AcrB of Escherichia coli.
  Proc Natl Acad Sci U S A, 107, 6559-6565.  
20676995 Y.Takatsuka, and H.Nikaido (2010).
Site-directed disulfide cross-linking to probe conformational changes of a transporter during its functional cycle: Escherichia coli AcrB multidrug exporter as an example.
  Methods Mol Biol, 634, 343-354.  
19695261 C.C.Su, F.Yang, F.Long, D.Reyon, M.D.Routh, D.W.Kuo, A.K.Mokhtari, J.D.Van Ornam, K.L.Rabe, J.A.Hoy, Y.J.Lee, K.R.Rajashankar, and E.W.Yu (2009).
Crystal structure of the membrane fusion protein CusB from Escherichia coli.
  J Mol Biol, 393, 342-355.
PDB codes: 3h94 3ooc 3opo 3ow7
18936189 C.Wehmeier, S.Schuster, E.Fähnrich, W.V.Kern, and J.A.Bohnert (2009).
Site-directed mutagenesis reveals amino acid residues in the Escherichia coli RND efflux pump AcrB that confer macrolide resistance.
  Antimicrob Agents Chemother, 53, 329-330.  
19136595 H.I.Zgurskaya (2009).
Covalently linked AcrB giant offers a new powerful tool for mechanistic analysis of multidrug efflux in bacteria.
  J Bacteriol, 191, 1727-1728.  
19722844 H.I.Zgurskaya (2009).
Multicomponent drug efflux complexes: architecture and mechanism of assembly.
  Future Microbiol, 4, 919-932.  
19026770 H.Nikaido, and Y.Takatsuka (2009).
Mechanisms of RND multidrug efflux pumps.
  Biochim Biophys Acta, 1794, 769-781.  
19231985 H.Nikaido (2009).
Multidrug resistance in bacteria.
  Annu Rev Biochem, 78, 119-146.  
18955484 H.T.Lin, V.N.Bavro, N.P.Barrera, H.M.Frankish, S.Velamakanni, H.W.van Veen, C.V.Robinson, M.I.Borges-Walmsley, and A.R.Walmsley (2009).
MacB ABC Transporter Is a Dimer Whose ATPase Activity and Macrolide-binding Capacity Are Regulated by the Membrane Fusion Protein MacA.
  J Biol Chem, 284, 1145-1154.  
19207745 J.L.Martinez, M.B.Sánchez, L.Martínez-Solano, A.Hernandez, L.Garmendia, A.Fajardo, and C.Alvarez-Ortega (2009).
Functional role of bacterial multidrug efflux pumps in microbial natural ecosystems.
  FEMS Microbiol Rev, 33, 430-449.  
19602147 J.Scherer, and D.H.Nies (2009).
CzcP is a novel efflux system contributing to transition metal resistance in Cupriavidus metallidurans CH34.
  Mol Microbiol, 73, 601-621.  
19254551 J.Weng, J.Ma, K.Fan, and W.Wang (2009).
Asymmetric conformational flexibility in the ATP-binding cassette transporter HI1470/1.
  Biophys J, 96, 1918-1930.  
19416927 K.M.Pos (2009).
Trinity revealed: Stoichiometric complex assembly of a bacterial multidrug efflux pump.
  Proc Natl Acad Sci U S A, 106, 6893-6894.  
19307562 K.Nagano, and H.Nikaido (2009).
Kinetic behavior of the major multidrug efflux pump AcrB of Escherichia coli.
  Proc Natl Acad Sci U S A, 106, 5854-5858.  
19329985 K.Nishino, Y.Senda, M.Hayashi-Nishino, and A.Yamaguchi (2009).
Role of the AraC-XylS family regulator YdeO in multi-drug resistance of Escherichia coli.
  J Antibiot (Tokyo), 62, 251-257.  
19996368 L.R.Forrest, and G.Rudnick (2009).
The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters.
  Physiology (Bethesda), 24, 377-386.  
19342493 M.F.Symmons, E.Bokma, E.Koronakis, C.Hughes, and V.Koronakis (2009).
The assembled structure of a complete tripartite bacterial multidrug efflux pump.
  Proc Natl Acad Sci U S A, 106, 7173-7178.
PDB code: 2v4d
19451626 N.Tal, and S.Schuldiner (2009).
A coordinated network of transporters with overlapping specificities provides a robust survival strategy.
  Proc Natl Acad Sci U S A, 106, 9051-9056.  
19383457 R.Schulz, and U.Kleinekathöfer (2009).
Transitions between closed and open conformations of TolC: the effects of ions in simulations.
  Biophys J, 96, 3116-3125.  
19278995 Smriti, P.Zou, and H.S.McHaourab (2009).
Mapping Daunorubicin-binding Sites in the ATP-binding Cassette Transporter MsbA Using Site-specific Quenching by Spin Labels.
  J Biol Chem, 284, 13904-13913.  
19453279 T.Eicher, L.Brandstätter, and K.M.Pos (2009).
Structural and functional aspects of the multidrug efflux pump AcrB.
  Biol Chem, 390, 693-699.  
18830684 T.von Rozycki, and D.H.Nies (2009).
Cupriavidus metallidurans: evolution of a metal-resistant bacterium.
  Antonie Van Leeuwenhoek, 96, 115-139.  
19678712 X.Z.Li, and H.Nikaido (2009).
Efflux-mediated drug resistance in bacteria: an update.
  Drugs, 69, 1555-1623.  
19060146 Y.Takatsuka, and H.Nikaido (2009).
Covalently linked trimer of the AcrB multidrug efflux pump provides support for the functional rotating mechanism.
  J Bacteriol, 191, 1729-1737.  
19788177 Z.Ma, F.E.Jacobsen, and D.P.Giedroc (2009).
Coordination chemistry of bacterial metal transport and sensing.
  Chem Rev, 109, 4644-4681.  
18535149 A.L.Davidson, E.Dassa, C.Orelle, and J.Chen (2008).
Structure, function, and evolution of bacterial ATP-binding cassette systems.
  Microbiol Mol Biol Rev, 72, 317.  
  18931428 D.Veesler, S.Blangy, C.Cambillau, and G.Sciara (2008).
There is a baby in the bath water: AcrB contamination is a major problem in membrane-protein crystallization.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 880-885.
PDB code: 3d9b
18379044 D.W.Li, M.Onishi, T.Kishino, T.Matsuo, W.Ogawa, T.Kuroda, and T.Tsuchiya (2008).
Properties and expression of a multidrug efflux pump AcrAB-KocC from Klebsiella pneumoniae.
  Biol Pharm Bull, 31, 577-582.  
18796513 E.Kilic, A.Spudich, U.Kilic, K.M.Rentsch, R.Vig, C.M.Matter, H.Wunderli-Allenspach, J.M.Fritschy, C.L.Bassetti, and D.M.Hermann (2008).
ABCC1: a gateway for pharmacological compounds to the ischaemic brain.
  Brain, 131, 2679-2689.  
18577510 E.Nikaido, A.Yamaguchi, and K.Nishino (2008).
AcrAB Multidrug Efflux Pump Regulation in Salmonella enterica serovar Typhimurium by RamA in Response to Environmental Signals.
  J Biol Chem, 283, 24245-24253.  
18707888 E.Padan (2008).
The enlightening encounter between structure and function in the NhaA Na+-H+ antiporter.
  Trends Biochem Sci, 33, 435-443.  
18024521 G.Krishnamoorthy, E.B.Tikhonova, and H.I.Zgurskaya (2008).
Fitting periplasmic membrane fusion proteins to inner membrane transporters: mutations that enable Escherichia coli AcrA to function with Pseudomonas aeruginosa MexB.
  J Bacteriol, 190, 691-698.  
18567659 H.Hirakawa, A.Takumi-Kobayashi, U.Theisen, T.Hirata, K.Nishino, and A.Yamaguchi (2008).
AcrS/EnvR represses expression of the acrAB multidrug efflux genes in Escherichia coli.
  J Bacteriol, 190, 6276-6279.  
18805970 H.Yamanaka, H.Kobayashi, E.Takahashi, and K.Okamoto (2008).
MacAB is involved in the secretion of Escherichia coli heat-stable enterotoxin II.
  J Bacteriol, 190, 7693-7698.  
18847219 I.Bagai, C.Rensing, N.J.Blackburn, and M.M.McEvoy (2008).
Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone.
  Biochemistry, 47, 11408-11414.  
18042544 I.Lehner, D.Basting, B.Meyer, W.Haase, T.Manolikas, C.Kaiser, M.Karas, and C.Glaubitz (2008).
The Key Residue for Substrate Transport (Glu14) in the EmrE Dimer Is Asymmetric.
  J Biol Chem, 283, 3281-3288.  
18849422 J.A.Bohnert, S.Schuster, M.A.Seeger, E.Fähnrich, K.M.Pos, and W.V.Kern (2008).
Site-directed mutagenesis reveals putative substrate binding residues in the Escherichia coli RND efflux pump AcrB.
  J Bacteriol, 190, 8225-8229.  
18793443 J.Wu, K.A.Hassan, R.A.Skurray, and M.H.Brown (2008).
Functional analyses reveal an important role for tyrosine residues in the staphylococcal multidrug efflux protein QacA.
  BMC Microbiol, 8, 147.  
18616285 K.M.Peters, J.T.Schuman, R.A.Skurray, M.H.Brown, R.G.Brennan, and M.A.Schumacher (2008).
QacR-cation recognition is mediated by a redundancy of residues capable of charge neutralization.
  Biochemistry, 47, 8122-8129.
PDB codes: 3bt9 3btc 3bti 3btj 3btl
18297445 K.Nishino, Y.Senda, and A.Yamaguchi (2008).
The AraC-family regulator GadX enhances multidrug resistance in Escherichia coli by activating expression of mdtEF multidrug efflux genes.
  J Infect Chemother, 14, 23-29.  
18835894 L.Vaccaro, K.A.Scott, and M.S.Sansom (2008).
Gating at both ends and breathing in the middle: conformational dynamics of TolC.
  Biophys J, 95, 5681-5691.  
18223659 M.A.Seeger, C.von Ballmoos, T.Eicher, L.Brandstätter, F.Verrey, K.Diederichs, and K.M.Pos (2008).
Engineered disulfide bonds support the functional rotation mechanism of multidrug efflux pump AcrB.
  Nat Struct Mol Biol, 15, 199-205.  
18812515 M.S.Wilke, M.Heller, A.L.Creagh, C.A.Haynes, L.P.McIntosh, K.Poole, and N.C.Strynadka (2008).
The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR.
  Proc Natl Acad Sci U S A, 105, 14832-14837.
PDB code: 3ech
19011636 T.Masaike, F.Koyama-Horibe, K.Oiwa, M.Yoshida, and T.Nishizaka (2008).
Cooperative three-step motions in catalytic subunits of F(1)-ATPase correlate with 80 degrees and 40 degrees substep rotations.
  Nat Struct Mol Biol, 15, 1326-1333.  
18076035 V.Cherezov, W.Liu, J.P.Derrick, B.Luan, A.Aksimentiev, V.Katritch, and M.Caffrey (2008).
In meso crystal structure and docking simulations suggest an alternative proteoglycan binding site in the OpcA outer membrane adhesin.
  Proteins, 71, 24-34.
PDB code: 2vdf
18406332 V.N.Bavro, Z.Pietras, N.Furnham, L.Pérez-Cano, J.Fernández-Recio, X.Y.Pei, R.Misra, and B.Luisi (2008).
Assembly and channel opening in a bacterial drug efflux machine.
  Mol Cell, 30, 114-121.
PDB codes: 2vdd 2vde
17210767 C.A.Elkins, and L.B.Mullis (2007).
Substrate competition studies using whole-cell accumulation assays with the major tripartite multidrug efflux pumps of Escherichia coli.
  Antimicrob Agents Chemother, 51, 923-929.  
17910961 C.C.Su, H.Nikaido, and E.W.Yu (2007).
Ligand-transporter interaction in the AcrB multidrug efflux pump determined by fluorescence polarization assay.
  FEBS Lett, 581, 4972-4976.  
17429392 C.F.Higgins (2007).
Multiple molecular mechanisms for multidrug resistance transporters.
  Nature, 446, 749-757.  
17194213 G.Sennhauser, P.Amstutz, C.Briand, O.Storchenegger, and M.G.Grütter (2007).
Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors.
  PLoS Biol, 5, e7.
PDB code: 2j8s
17893146 I.Bagai, W.Liu, C.Rensing, N.J.Blackburn, and M.M.McEvoy (2007).
Substrate-linked conformational change in the periplasmic component of a Cu(I)/Ag(I) efflux system.
  J Biol Chem, 282, 35695-35702.  
17933888 K.Nishino, E.Nikaido, and A.Yamaguchi (2007).
Regulation of multidrug efflux systems involved in multidrug and metal resistance of Salmonella enterica serovar Typhimurium.
  J Bacteriol, 189, 9066-9075.  
17159924 O.Lomovskaya, H.I.Zgurskaya, M.Totrov, and W.J.Watkins (2007).
Waltzing transporters and 'the dance macabre' between humans and bacteria.
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17360572 S.Lobedanz, E.Bokma, M.F.Symmons, E.Koronakis, C.Hughes, and V.Koronakis (2007).
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PDB code: 2rdd
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Organization of reconstituted lipoprotein MexA onto supported lipid membrane.
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Structural biology: the ins and outs of drug transport.
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The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.