X-ray structure of the metal-sensor CnrX in both the apo- and copper-bound forms

FEBS Letters

Volumn 582, Issue 28, 2008, Pages 3954-3958

  Pompidor, Guillaume ^a   Maillard, Antoine P ^a   Girard, Eric ^a   Gambarelli, Serge ^b   Kahn, Richard ^a   Covès, Jacques ^a  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^b UNIV GRENOBLE ALPES   (France)

Author keywords

CnrX; Cupriavidus metallidurans CH34; Heavy metal; Metal sensor; Signal transduction; X ray structure

Indexed keywords

BACTERIAL PROTEIN; COPPER; PROTEIN CNRX; SELENOMETHIONINE; SULFUR; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL STRUCTURE; CONFORMATIONAL TRANSITION; CUPRIAVIDUS; CUPRIAVIDUS METALLIDURANS; METAL BINDING; METALLATION; PRIORITY JOURNAL; SENSOR; SIGNAL TRANSDUCTION; X RAY ANALYSIS;

AMINO ACID SEQUENCE; APOPROTEINS; BACTERIAL PROTEINS; COPPER; CRYSTALLOGRAPHY, X-RAY; CUPRIAVIDUS; DIMERIZATION; MOLECULAR SEQUENCE DATA; PERIPLASMIC PROTEINS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY;

CUPRIAVIDUS METALLIDURANS;

EID: 56049087926     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.10.042     Document Type: Article

References (40)

1. Raivio T.L., and Silhavy T.J. Periplasmic stress and ECF sigma factors. Annu. Rev. Microbiol. 55 (2001) 591-624
2. Alba B.M., and Gross C.A. Regulation of the Escherichia coli sigma-dependent envelope stress response. Mol. Microbiol. 52 (2004) 613-619
3. Ades S.E. Control of the alternative sigma factor sigmaE in Escherichia coli. Curr. Opin. Microbiol. 7 (2004) 157-162
4. Helmann J.D. The extracytoplasmic function (ECF) sigma factors. Adv. Microb. Physiol. 46 (2002) 47-110
5. Paget M.S., and Helmann J.D. The sigma70 family of sigma factors. Genome Biol. 4 (2003) 203
6. Mergeay M., Monchy S., Vallaeys T., Auquier V., Benotmane M.A., Bertin P., Taghavi S., Dunn J., van der Lelie D., and Wattiez R. Ralstonia metallidurans, a bacterium specifically adapted to toxic metals: towards a catalogue of metal-responsive genes. FEMS Microbiol. Rev. 27 (2003) 385-410
7. Monchy S., Benotmane M.A., Janssen P., Vallaeys T., Taghavi S., van der Lelie D., and Mergeay M. Plasmids pMOL28 and pMOL30 of Cupriavidus metallidurans are specialized in the maximal viable response to heavy metals. J. Bacteriol. 189 (2007) 7417-7425
8. Nies D.H. Incidence and function of sigma factors in Ralstonia metallidurans and other bacteria. Arch. Microbiol. 181 (2004) 255-268
9. Grosse C., Friedrich S., and Nies D.H. Contribution of extracytoplasmic function sigma factors to transition metal homeostasis in Cupriavidus metallidurans strain CH34. J. Mol. Microbiol. Biotechnol. 12 (2007) 227-240
10. Nies D.H. Efflux-mediated heavy metal resistance in prokaryotes. FEMS Microbiol. Rev. 27 (2003) 313-339
11. Liesegang H., Lemke K., Siddiqui R.A., and Schlegel H.G. Characterization of the inducible nickel and cobalt resistance determinant cnr from pMOL28 of Alcaligenes eutrophus CH34. J. Bacteriol. 175 (1993) 767-778
12. Tibazarwa C., Wuertz S., Mergeay M., Wyns L., and van der Lelie D. Regulation of the cnr cobalt and nickel resistance determinant of Ralstonia eutropha (Alcaligenes eutrophus) CH34. J. Bacteriol. 182 (2000) 1399-1409
13. Grass G., Grosse C., and Nies D.H. Regulation of the cnr cobalt and nickel resistance determinant from Ralstonia sp. strain CH34. J. Bacteriol. 182 (2000) 1390-1398
14. Grass G., Fricke B., and Nies D.H. Control of expression of a periplasmic nickel efflux pump by periplasmic nickel concentrations. Biometals 18 (2005) 437-448
15. Pompidor, G., Girard, E., Maillard, A., Ramella-Pairin, S., Bersch. B., Kahn, R. and Covès, J. (in press) Biostructural analysis of the metal-sensor domain of CnrX from Cupriavidus metallidurans CH34. Anthonie van Leeuvenhoek. doi: 10.1007/s10482-008-9283-6.
16. Van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., and Clardy J. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229 (1993) 105-124
17. Kabsch W. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Cryst. 21 (1988) 916-924
18. Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Cryst. D50, 760-763.
19. De la Fortelle E., and Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction. Meth. Enzymol. 276 (1997) 472-494
20. Schneider T.R., and Scheldrick G.M. Substructure solution with SHELXD. Acta Cryst. D58 (2002) 1772-1779
21. 1 ATPase. Acta Cryst. D52 (1996) 30-42
22. Cowtan K.D., and Main P. Phase combination and cross validation in iterated density-modification calculations. Acta Cryst. D52 (1996) 43-48
23. Lamzin V.S., Perrakis A., and Wilson K.S. The ARP/WARP suite for automated construction and refinement of protein models. In: Rossman M.G., and Arnold E. (Eds). Int. Tables for Crystallography. Vol. F: Crystallography of Biological Macromolecules, Dordrecht (2001), Kluwer Academic Publishers, The Netherlands 720-722
24. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst. D53 (1997) 240-255
25. Brünger A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355 (1992) 472-475
26. Jones S., and Thornton J.M. Principles of protein-protein interactions. Proc. Natl. Acad. Sci. USA 93 (1996) 13-20
27. Peisach J., and Blumberg W.E. Structural implications derived from the analysis of electron paramagnetic resonance-spectra of natural and artificial copper proteins. Arch. Biochem. Biophys. 165 (1974) 691-708
28. Gibrat J.F., Madej T., and Bryant S.H. Surprising similarities in structure comparison. Curr. Opin. Struct. Biol. 6 (1996) 377-385
29. Holm L., and Sander C. Mapping the protein universe. Science 273 (1996) 595-603
30. Koch K.A., Peña M.M., and Thiele D.J. Copper-binding motifs in catalysis, transport, detoxification and signaling. Chem. Biol. 4 (1997) 549-560
31. Diederix R.E., Canters G.W., and Dennison C. The Met99Gln mutant of amicyanin form Paracoccus versutus. Biochemistry 39 (2000) 9551-9560
32. Berry S.M., Ralle M., Low D.W., Blackburn N.J., and Lu Y. Probing the role of axial methionine in the blue copper center of azurin with unnatural amino acids. J. Am. Chem. Soc. 125 (2003) 8760-8768
33. Bauer R., Danielsen E., Hemmingsen L., Bjerrum M.J., Hansson O., and Singh K. Interplay between oxidation state and coordination geometry of metal ions in azurin. J. Am. Chem. Soc. 119 (1997) 157-162
34. Ehrmann M., and Clausen T. Proteolysis as a regulatory mechanism. Annu. Rev. Genet. 38 (2004) 709-724
35. Brooks B.E., and Buchanan S.K. Signaling mechanisms for activation of extracytoplasmic function (ECF) sigma factors. Biochim. Biophys. Acta 1778 (2008) 1930-1945
36. Gomis-Rüth F.X., Grams F., Yiallouros I., Nar H., Küsthardt U., Zwilling R., Bode W., and Stöcker W. Crystal structures, spectroscopic features, and catalytic properties of cobalt(II), copper(II), nickel(II), and mercury(II) derivatives of the zinc endopeptidase astacin. A correlation of structure and proteolytic activity. J. Biol. Chem. 269 (1994) 17111-17117
37. Pettersen E.F., Goddard T.D., Huang C.C., Couch G.S., Greenblatt D.M., Meng E.C., and Ferrin T.E. UCSF chimera - a visualization system for exploratory research and analysis. J. Comput. Chem. 25 (2004) 1605-1612
38. Krissinel E., and Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372 (2007) 774-797
39. Plewniak F., Bianchetti L., Brelivet Y., Carles A., Chalmel F., Lecompte O., Mochel T., Moulinier L., Muller A., Muller J., Prigent V., Ripp R., Thierry J.-C., Thompson J.D., Wicker N., and Poch O. PipeAlign: a new toolkit for protein family analysis. Nucl. Acid Res. 31 (2003) 3829-3832
40. Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The ClustalX windows interface. Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl. Acid Res. 25 (1997) 4876-4882