Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump

PLoS ONE

Volumn 6, Issue 1, 2011, Pages

  Kulathila, Rithika ^a   Kulathila, Ragini ^a   Indic, Mridhu ^a   van den Berg, Bert ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; OUTER MEMBRANE PROTEIN; PROTEIN CUSC; SILVER; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; HEAVY METAL; IBE10 PROTEIN, E COLI; MEMBRANE PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL CELL; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENE AMPLIFICATION; NONHUMAN; PROTEIN EXPRESSION; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ESCHERICHIA COLI;

COPPER; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; METALS, HEAVY; MODELS, MOLECULAR; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SILVER; SUBSTRATE SPECIFICITY;

EID: 79251563176     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0015610     Document Type: Article

References (29)

1. Rensing C, Grass G (2003) Escherichia coli mechanisms of copper homeostasis in a changing environment. FEMS Microbiol Rev 27: 197-213.
2. Franke S, Grass G, Rensing C, Nies DH (2003) Molecular analysis of the copper- transporting efflux system CusCFBA of Escherichia coli. J Bacteriol 185: 3804-3812.
3. Nies DH (2003) Efflux-mediated heavy metal resistance in prokaryotes. FEMS Microbiol Rev 27: 313-339.
4. Paulsen IT, Park JH, Choi PS, Saier MH, Jr. (1997) A family of gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from gram-negative bacteria. FEMS Microbiol Lett 156: 1-8.
5. Kittleson JT, Loftin IR, Hausrath AC, Engelhardt KP, Rensing C, et al. (2006) Periplasmic metal-resistance protein CusF exhibits high affinity and specificity for both CuI and AgI. Biochemistry 45: 11096-11102.
6. Loftin IR, Franke S, Blackburn NJ, McEvoy MM (2007) Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy. Protein Sci 16: 2287-2293.
7. Bagai I, Rensing C, Blackburn NJ, McEvoy MM (2008) Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone. Biochemistry 47: 11408-11414.
8. Murakami S, Nakashima R, Yamashita E, Yamaguchi A (2002) Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419: 587-593.
9. Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A (2006) Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443: 173-179.
10. Nikaido H, Takatsuka Y (2009) Mechanisms of RND multidrug efflux pumps. Biochim Biophys Acta 1794: 769-781.
11. Mikolosko J, Bobyk K, Zgurskaya HI, Ghosh P (2006) Conformational flexibility in the multidrug efflux system protein AcrA. Structure 14: 577-587.
12. Symmons MF, Bokma E, Koronakis E, Hughes C, Koronakis V (2009) The assembled structure of a complete tripartite bacterial multidrug efflux pump. Proc Natl Acad Sci U S A 106: 7173-7178.
13. Koronakis V, Sharff A, Koronakis E, Luisi B, Hughes C (2001) Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405: 914-919.
14. Bavro VN, Pietras Z, Furnham N, Pe ́rez-Cano L, Ferna ́ndez-Recio J, et al. (2008) Assembly and channel opening in a bacterial drug efflux machine. Mol Cell 30: 114-121.
15. Su CC, Yang F, Long F, Reyon D, Routh MD, et al. (2009) Crystal structure of the membrane fusion protein CusB from Escherichia coli. J Mol Biol 393: 342-355.
16. Xue Y, Davis AV, Balakrishnan G, Stasser JP, Staehlin BM, et al. (2008) Cu(I) recognition via cation-pi and methionine interactions in CusF. Nat Chem Biol 4: 107-109.
17. Long F, Su CC, Zimmermann MT, Boyken SE, Rajashankar KR, et al. (2010) Crystal structures of the CusA efflux pump suggest methionine- mediated metal transport. Nature 467: 484-488.
18. Deniaud A, Goulielmakis A, Coves J, Pebay-Peyroula E (2009) Differences between CusA and AcrB crystallisation highlighted by protein flexibility. PLoS One 4: e6214.
19. Su CC, Long F, Yu EW (2010) The cus efflux system removes toxic ions via a methionine shuttle. Protein Sci, Oct 27. [Epub ahead of print].
20. Conroy O, Kim EH, McEvoy MM, Rensing C (2010) Differing ability to transport nonmetal substrates by two RND-type metal exporters. FEMS Microbiol Lett 308: 115-122.
21. The PyMOL Molecular Graphics System, Version 1.3, Schrödinger, LLC.
22. Neilsen PO, Zimmerman GA, McIntyre TM (2001) Escherichia coli Braun lipoprotein induces a lipopolysaccharide-like endotoxic response from primary human endothelial cells. J Immunol 167: 5231-5239.
23. Akama H, Kanemaki M, Yoshimura M, Tsukihara T, Kashiwagi T, et al. (2004) Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end. J Biol Chem 279: 52816-52819.
24. Guzman L, Belin D, Carson M, Beckwith J (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177: 4121-4130.
25. Haun RS, Moss J (1992) Ligation-independent cloning of glutathione Stransferase fusion genes for expression in Escherichia coli. Gene 112: 37-43.
26. Otwinowski Z, Minor W (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode. Methods in Enzymology, Volume 276: Macromolecular Crystallography. Methods Enzymol 276: 307-326.
27. Collaborative Computational Project, N (1994) The Ccp4 suite-programs for protein crystallography. Acta Cryst D50: 760-763.
28. Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallographica Section D 60: 2126-2132.
29. Zwart PH, Afonine PV, Grosse-Kunstleve RW, Hung L-W, Ioerger TR, et al. (2008) Automated Structure Solution with the PHENIX Suite. In: Kobe B, Guss M, Huber T, eds. Methods in Molecular Biology Humana Press. Pp 419-435.