Structural characterization and biological implications of di-zinc binding in the ferroxidase center of Streptococcus pyogenes Dpr

Biochemical and Biophysical Research Communications

Volumn 398, Issue 3, 2010, Pages 361-365

  Haikarainen, Teemu ^a   Tsou, Chih Cheng ^b   Wu, Jiunn Jong ^b   Papageorgiou, Anastassios C ^a  

^a UNIVERSITY OF TURKU   (Finland)

^b NATIONAL CHENG KUNG UNIVERSITY   (Taiwan)

Author keywords

Fenton reaction; Ferritins; Ferroxidase; Hydrogen peroxide; Oxidative stress; Streptococcal proteins; Zinc

Indexed keywords

BACTERIAL PROTEIN; CERULOPLASMIN; FERRITIN; HYDROGEN PEROXIDE; MEMBRANE PROTEIN; ZINC; ZINC BINDING PROTEIN;

ARTICLE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; FENTON REACTION; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN STRUCTURE; STREPTOCOCCUS PYOGENES;

BACTERIAL PROTEINS; BINDING SITES; CERULOPLASMIN; CRYSTALLOGRAPHY, X-RAY; DNA-BINDING PROTEINS; PROTEIN CONFORMATION; STREPTOCOCCUS PYOGENES; ZINC;

STREPTOCOCCUS PYOGENES;

EID: 77955276650     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.06.071     Document Type: Article

References (30)

1. Haikarainen T., Papageorgiou A. Dps-like proteins: structural and functional insights into a versatile protein family. Cell. Mol. Life Sci. 2010, 67:341-351.
2. Chiancone E., Ceci P. The multifaceted capacity of Dps proteins to combat bacterial stress conditions: detoxification of iron and hydrogen peroxide and DNA binding. Biochim. Biophys. Acta 2010, 1800:798-805.
3. Almiron M., Link A.J., Furlong D., Kolter R. A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev. 1992, 6:2646-2654.
4. Ceci P., Mangiarotti L., Rivetti C., Chiancone E. The neutrophil-activating Dps protein of Helicobacter pylori, HP-NAP, adopts a mechanism different from Escherichia coli Dps to bind and condense DNA. Nucleic Acids Res. 2007, 35:2247-2256.
5. Havukainen H., Haataja S., Kauko A., Pulliainen A.T., Salminen A., Haikarainen T., Finne J., Papageorgiou A.C. Structural basis of the zinc- and terbium-mediated inhibition of ferroxidase activity in Dps ferritin-like proteins. Protein Sci. 2008, 17:1513-1521.
6. Romao C.V., Mitchell E.P., McSweeney S. The crystal structure of Deinococcus radiodurans Dps protein (DR2263) reveals the presence of a novel metal centre in the N terminus. J. Biol. Inorg. Chem. 2006, 11:891-902.
7. Stillman T.J., Upadhyay M., Norte V.A., Sedelnikova S.E., Carradus M., Tzokov S., Bullough P.A., Shearman C.A., Gasson M.J., Williams C.H., Artymiuk P.J., Green J. The crystal structures of Lactococcus lactis MG1363 Dps proteins reveal the presence of an N-terminal helix that is required for DNA binding. Mol. Microbiol. 2005, 57:1101-1112.
8. Ilari A., Ceci P., Ferrari D., Rossi G.L., Chiancone E. Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core. J. Biol. Chem. 2002, 277:37619-37623.
9. Grant R.A., Filman D.J., Finkel S.E., Kolter R., Hogle J.M. The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat. Struct. Biol. 1998, 5:294-303.
10. Franceschini S., Ceci P., Alaleona F., Chiancone E., Ilari A. Antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus. FEBS J. 2006, 273:4913-4928.
11. Ilari A., Stefanini S., Chiancone E., Tsernoglou D. The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site. Nat. Struct. Biol. 2000, 7:38-43.
12. Kauko A., Pulliainen A.T., Haataja S., Meyer-Klaucke W., Finne J., Papageorgiou A.C. Iron incorporation in Streptococcus suis Dps-like peroxide resistance protein Dpr requires mobility in the ferroxidase center and leads to the formation of a ferrihydrite-like core. J. Mol. Biol. 2006, 364:97-109.
13. Roy S., Gupta S., Das S., Sekar K., Chatterji D., Vijayan M. X-ray analysis of Mycobacterium smegmatis Dps and a comparative study involving other Dps and Dps-like molecules. J. Mol. Biol. 2004, 339:1103-1113.
14. Ceci P., Ilari A., Falvo E., Chiancone E. The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties. J. Biol. Chem. 2003, 278:20319-20326.
15. Ren B., Tibbelin G., Kajino T., Asami O., Ladenstein R. The multi-layered structure of Dps with a novel di-nuclear ferroxidase center. J. Mol. Biol. 2003, 329:467-477.
16. Zeth K., Offermann S., Essen L.O., Oesterhelt D. Iron-oxo clusters biomineralizing on protein surfaces: structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states. Proc. Natl. Acad. Sci. USA 2004, 101:13780-13785.
17. Alaleona F., Franceschini S., Ceci P., Ilari A., Chiancone E. Thermosynechoccus elongatus DpsA binds Zn(II) at a unique three histidine-containing ferroxidase center and utilizes O(2) as iron oxidant with very high efficiency, unlike the typical Dps proteins. FEBS J. 2010, 277:903-917.
18. Tsou C.C., Chiang-Ni C., Lin Y.S., Chuang W.J., Lin M.T., Liu C.C., Wu J.J. An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses. Infect. Immun. 2008, 76:4038-4045.
19. Tsou C., Chiang-Ni C., Lin Y., Chuang W., Lin M., Liu C., Wu J. Oxidative stress and metal ions regulate a ferritin-like gene, Dpr, in Streptococcus pyogenes. Int. J. Med. Microbiol. 2010, 300:259-264.
20. Haikarainen T., Tsou C.C., Wu J.J., Papageorgiou A.C. Crystal structures of Streptococcus pyogenes Dpr reveal a dodecameric iron-binding protein with a ferroxidase site. J. Biol. Inorg. Chem. 2010, 15:183-194.
21. Leslie A.G. The integration of macromolecular diffraction data. Acta Crystallogr. D Biol. Crystallogr. 2006, 62:48-57.
22. The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763.
23. Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 1997, 53:240-255.
24. Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 2004, 60:2126-2132.
25. 2+ site in the Bacillus subtilis peroxide sensor PerR. J. Biol. Chem. 2006, 281:23567-23578.
26. Stillman T.J., Hempstead P.D., Artymiuk P.J., Andrews S.C., Hudson A.J., Treffry A., Guest J.R., Harrison P.M. The high-resolution X-ray crystallographic structure of the ferritin (EcFtnA) of Escherichia coli; comparison with human H ferritin (HuHF) and the structures of the Fe(3+) and Zn(2+) derivatives. J. Mol. Biol. 2001, 307:587-603.
27. Versieck J. Trace elements in human body fluids and tissues. Crit. Rev. Clin. Lab. Sci. 1985, 22:97-184.
28. Milanino R., Marrella M., Gasperini R., Pasqualicchio M., Velo G. Copper and zinc body levels in inflammation: an overview of the data obtained from animal and human studies. Agents Actions 1993, 39:195-209.
29. Yamamoto Y., Poole L.B., Hantgan R.R., Kamio Y. An iron-binding protein, Dpr, from Streptococcus mutans prevents iron-dependent hydroxyl radical formation in vitro. J. Bacteriol. 2002, 184:2931-2939.
30. Weiss M. Global indicators of X-ray data quality. J Appl Cryst 2001, 34:130-135.