Crystal structure of human copper homeostasis protein CutC reveals a potential copper-binding site

Journal of Structural Biology

Volumn 169, Issue 3, 2010, Pages 399-405

  Li, Yingjie ^a,b   Du, Jiamu ^a   Zhang, Peng ^a   Ding, Jianping ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

Conserved sequence motif; Copper homeostasis protein; Crystal structure; CutC; Metal binding site

Indexed keywords

COPPER PROTEIN; CYSTEINE; PROTEIN CUTC; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; BIOCHEMISTRY; CONTROLLED STUDY; CRYSTAL STRUCTURE; HUMAN; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BINDING SITES; CATION TRANSPORT PROTEINS; COPPER; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; X-RAY DIFFRACTION;

BACTERIA (MICROORGANISMS);

EID: 77049089212     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.10.012     Document Type: Article

References (33)

1. Arnesano F., Banci L., Bertini I., Ciofi-Baffoni S., Molteni E., Huffman D.L., and O'Halloran T.V. Metallochaperones and metal-transporting ATPases: a comparative analysis of sequences and structures. Genome Res. 12 (2002) 255-271
2. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
3. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., and Warren G.L. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54 (1998) 905-921
4. Calafato S., Swain S., Hughes S., Kille P., and Sturzenbaum S.R. Knockdown of Caenorhabditis elegans cutc-1 exacerbates the sensitivity towards high levels of copper. Toxicol. Sci. 106 (2008) 7
5. CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50 (1994) 760-763
6. Changela A., Chen K., Xue Y., Holschen J., Outten C.E., O'Halloran T.V., and Mondragon A. Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR. Science 301 (2003) 1383-1387
7. DiDonato M., and Sarkar B. Copper transport and its alterations in Menkes and Wilson diseases. Biochim. Biophys. Acta 1360 (1997) 3-16
8. Doukov T.I., Iverson T.M., Seravalli J., Ragsdale S.W., and Drennan C.L. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science 298 (2002) 567-572
9. Finney L.A., and O'Halloran T.V. Transition metal speciation in the cell: insights from the chemistry of metal ion receptors. Science 300 (2003) 931-936
10. Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
11. Gupta S.D., Lee B.T., Camakaris J., and Wu H.C. Identification of cutC and cutF (nlpE) genes involved in copper tolerance in Escherichia coli. J. Bacteriol. 177 (1995) 4207-4215
12. Huffman D.L., and O'Halloran T.V. Function, structure, and mechanism of intracellular copper trafficking proteins. Annu. Rev. Biochem. 70 (2001) 677-701
13. Jensen P.Y., Bonander N., Horn N., Tumer Z., and Farver O. Expression, purification and copper-binding studies of the first metal-binding domain of Menkes protein. Eur. J. Biochem. 264 (1999) 890-896
14. Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
15. Kimura T., and Nishioka H. Intracellular generation of superoxide by copper sulphate in Escherichia coli. Mutat. Res. 389 (1997) 237-242
16. Laskowski R.A., Macarthur M.W., Moss D.S., and Thornton J.M. Procheck-a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26 (1993) 283-291
17. Lee J., Prohaska J.R., and Thiele D.J. Essential role for mammalian copper transporter Ctr1 in copper homeostasis and embryonic development. Proc. Natl. Acad. Sci. USA 98 (2001) 6842-6847
18. Li J., Ji C., Chen J., Yang Z., Wang Y., Fei X., Zheng M., Gu X., Wen G., Xie Y., and Mao Y. Identification and characterization of a novel Cut family cDNA that encodes human copper transporter protein CutC. Biochem. Biophys. Res. Commun. 337 (2005) 179-183
19. Liu T., Ramesh A., Ma Z., Ward S.K., Zhang L., George G.N., Talaat A.M., Sacchettini J.C., and Giedroc D.P. CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulator. Nat. Chem. Biol. 3 (2007) 60-68
20. Mao M., Fu G., Wu J.S., Zhang Q.H., Zhou J., Kan L.X., Huang Q.H., He K.L., Gu B.W., Han Z.G., Shen Y., Gu J., Yu Y.P., Xu S.H., Wang Y.X., Chen S.J., and Chen Z. Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning. Proc. Natl. Acad. Sci. USA 95 (1998) 8175-8180
21. Odermatt A., Suter H., Krapf R., and Solioz M. Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J. Biol. Chem. 268 (1993) 12775-12779
22. Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., et al. Complete sequencing and characterization of 21, 243 full-length human cDNAs. Nat. Genet. 36 (2004) 40-45
23. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
24. Pena M.M., Lee J., and Thiele D.J. A delicate balance: homeostatic control of copper uptake and distribution. J. Nutr. 129 (1999) 1251-1260
25. Rae T.D., Schmidt P.J., Pufahl R.A., Culotta V.C., and O'Halloran T.V. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 284 (1999) 805-808
26. Rensing C., and Grass G. Escherichia coli mechanisms of copper homeostasis in a changing environment. FEMS Microbiol. Rev. 27 (2003) 197-213
27. Rosenzweig A.C., Huffman D.L., Hou M.Y., Wernimont A.K., Pufahl R.A., and O'Halloran T.V. Crystal structure of the Atx1 metallochaperone protein at 1.02 Å resolution. Structure 7 (1999) 605-617
28. Schaefer M., and Gitlin J.D. Genetic disorders of membrane transport. IV. Wilson's disease and Menkes disease. Am. J. Physiol. 276 (1999) G311-G314
29. Silver S., and Phung L.T. Bacterial heavy metal resistance: new surprises. Annu. Rev. Microbiol. 50 (1996) 753-789
30. Wierenga R.K. The TIM-barrel fold: a versatile framework for efficient enzymes. FEBS Lett. 492 (2001) 193-198
31. Xiao Z., Loughlin F., George G.N., Howlett G.J., and Wedd A.G. C-terminal domain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu(I) ions as a cuprous-thiolate polynuclear cluster: sub-femtomolar Cu(I) affinity of three proteins involved in copper trafficking. J. Am. Chem. Soc. 126 (2004) 3081-3090
32. Zhou L., Singleton C., and Le Brun N.E. High Cu(I) and low proton affinities of the CXXC motif of Bacillus subtilis CopZ. Biochem. J. 413 (2008) 459-465
33. Zhu D.Y., Zhu Y.Q., Huang R.H., Xiang Y., Yang N., Lu H.X., Li G.P., Jin Q., and Wang D.C. Crystal structure of the copper homeostasis protein (CutCm) from Shigella flexneri at 1.7 Å resolution: the first structure of a new sequence family of TIM barrels. Proteins 58 (2005) 764-768