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Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist.

Törnroth-Horsefield S, Gourdon P, Horsefield R, Brive L, Yamamoto N, Mori H, Snijder A, Neutze R
Structure 15 1663-73 (2007)
Cited: 57 times
EuropePMC logo PMID: 18073115

Abstract

Bacterial drug resistance is a serious concern for human health. Multidrug efflux pumps export a broad variety of substrates out of the cell and thereby convey resistance to the host. In Escherichia coli, the AcrB:AcrA:TolC efflux complex forms a principal transporter for which structures of the individual component proteins have been determined in isolation. Here, we present the X-ray structure of AcrB in complex with a single transmembrane protein, assigned by mass spectrometry as YajC. A specific rotation of the periplasmic porter domain of AcrB is also revealed, consistent with the hypothesized "twist-to-open" mechanism for TolC activation. Growth experiments with yajc-deleted E. coli reveal a modest increase in the organism's susceptibility to beta-lactam antibiotics, but this effect could not conclusively be attributed to the loss of interactions between YajC and AcrB.

Reviews - 2rdd mentioned but not cited (2)

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Articles - 2rdd mentioned but not cited (4)

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Reviews citing this publication (23)

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Articles citing this publication (28)

  1. Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket. Nakashima R, Sakurai K, Yamasaki S, Nishino K, Yamaguchi A. Nature 480 565-569 (2011)
  2. Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop. Eicher T, Cha HJ, Seeger MA, Brandstätter L, El-Delik J, Bohnert JA, Kern WV, Verrey F, Grütter MG, Diederichs K, Pos KM. Proc Natl Acad Sci U S A 109 5687-5692 (2012)
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  4. Conserved small protein associates with the multidrug efflux pump AcrB and differentially affects antibiotic resistance. Hobbs EC, Yin X, Paul BJ, Astarita JL, Storz G. Proc Natl Acad Sci U S A 109 16696-16701 (2012)
  5. A mecA-negative strain of methicillin-resistant Staphylococcus aureus with high-level β-lactam resistance contains mutations in three genes. Banerjee R, Gretes M, Harlem C, Basuino L, Chambers HF. Antimicrob Agents Chemother 54 4900-4902 (2010)
  6. The structure of the efflux pump AcrB in complex with bile acid. Drew D, Klepsch MM, Newstead S, Flaig R, De Gier JW, Iwata S, Beis K. Mol Membr Biol 25 677-682 (2008)
  7. Cryo-Electron Microscopy Structure of an Acinetobacter baumannii Multidrug Efflux Pump. Su CC, Morgan CE, Kambakam S, Rajavel M, Scott H, Huang W, Emerson CC, Taylor DJ, Stewart PL, Bonomo RA, Yu EW. mBio 10 e01295-19 (2019)
  8. Structural and dynamical insights into the opening mechanism of P. aeruginosa OprM channel. Phan G, Benabdelhak H, Lascombe MB, Benas P, Rety S, Picard M, Ducruix A, Etchebest C, Broutin I. Structure 18 507-517 (2010)
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  10. Transport of lipophilic carboxylates is mediated by transmembrane helix 2 in multidrug transporter AcrB. Oswald C, Tam HK, Pos KM. Nat Commun 7 13819 (2016)
  11. Effects of zinc on particulate methane monooxygenase activity and structure. Sirajuddin S, Barupala D, Helling S, Marcus K, Stemmler TL, Rosenzweig AC. J Biol Chem 289 21782-21794 (2014)
  12. Evolution of amoxicillin resistance of Helicobacter pylori in vitro: characterization of resistance mechanisms. Qureshi NN, Gallaher B, Schiller NL. Microb Drug Resist 20 509-516 (2014)
  13. Three ways in, one way out: water dynamics in the trans-membrane domains of the inner membrane translocase AcrB. Fischer N, Kandt C. Proteins 79 2871-2885 (2011)
  14. Some ligands enhance the efflux of other ligands by the Escherichia coli multidrug pump AcrB. Kinana AD, Vargiu AV, Nikaido H. Biochemistry 52 8342-8351 (2013)
  15. Transitions between closed and open conformations of TolC: the effects of ions in simulations. Schulz R, Kleinekathöfer U. Biophys J 96 3116-3125 (2009)
  16. Crystal structure of AcrB complexed with linezolid at 3.5 Å resolution. Hung LW, Kim HB, Murakami S, Gupta G, Kim CY, Terwilliger TC. J Struct Funct Genomics 14 71-75 (2013)
  17. Structural mechanisms of heavy-metal extrusion by the Cus efflux system. Delmar JA, Su CC, Yu EW. Biometals 26 593-607 (2013)
  18. Characterization of the RND family of multidrug efflux pumps: in silico to in vivo confirmation of four functionally distinct subgroups. Godoy P, Molina-Henares AJ, de la Torre J, Duque E, Ramos JL. Microb Biotechnol 3 691-700 (2010)
  19. Secretome analysis defines the major role of SecDF in Staphylococcus aureus virulence. Quiblier C, Seidl K, Roschitzki B, Zinkernagel AS, Berger-Bächi B, Senn MM. PLoS One 8 e63513 (2013)
  20. AcrB trimer stability and efflux activity, insight from mutagenesis studies. Yu L, Lu W, Wei Y. PLoS One 6 e28390 (2011)
  21. Escherichia coli as host for membrane protein structure determination: a global analysis. Hattab G, Warschawski DE, Moncoq K, Miroux B. Sci Rep 5 12097 (2015)
  22. Mapping the Dynamic Functions and Structural Features of AcrB Efflux Pump Transporter Using Accelerated Molecular Dynamics Simulations. Jamshidi S, Sutton JM, Rahman KM. Sci Rep 8 10470 (2018)
  23. Elastic network model-based normal mode analysis reveals the conformational couplings in the tripartite AcrAB-TolC multidrug efflux complex. Wang B, Weng J, Fan K, Wang W. Proteins 79 2936-2945 (2011)
  24. A Screen for Antibiotic Resistance Determinants Reveals a Fitness Cost of the Flagellum in Pseudomonas aeruginosa. Rundell EA, Commodore N, Goodman AL, Kazmierczak BI. J Bacteriol 202 e00682-19 (2020)
  25. Dissecting the function of a protruding loop in AcrB trimerization. Fang J, Yu L, Wu M, Wei Y. J Biomol Struct Dyn 31 385-392 (2013)
  26. Functional relevance of AcrB Trimerization in pump assembly and substrate binding. Lu W, Zhong M, Chai Q, Wang Z, Yu L, Wei Y. PLoS One 9 e89143 (2014)
  27. Probing the Dynamics of AcrB Through Disulfide Bond Formation. Rajapaksha P, Pandeya A, Wei Y. ACS Omega 5 21844-21852 (2020)
  28. In Vitro Microevolution and Co-Selection Assessment of Florfenicol Impact on Escherichia coli Resistance Development. Kerek Á, Török B, Laczkó L, Kardos G, Bányai K, Somogyi Z, Kaszab E, Bali K, Jerzsele Á. Antibiotics (Basel) 12 1728 (2023)


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