Structure of Cu/Zn superoxide dismutase from the heavy-metal-tolerant yeast Cryptococcus liquefaciens strain N6

Biochemical and Biophysical Research Communications

Volumn 374, Issue 3, 2008, Pages 475-478

  Teh, Aik Hong ^a   Kanamasa, Shin ^b,c   Kajiwara, Susumu ^b   Kumasaka, Takashi ^a,b  

^a JAPAN SYNCHROTRON RADIATION RESEARCH INSTITUTE   (Japan)

^b TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^c CHUBU UNIVERSITY   (Japan)

Author keywords

Copper; Crystal structure; Cu Zn superoxide dismutase; Electrostatic loop; Structural stabilization

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; GLYCINE; HISTIDINE; PROLINE; THREONINE;

AMINO ACID SUBSTITUTION; ARTICLE; CRYPTOCOCCUS; CRYPTOCOCCUS LIQUEFACIENS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; FUNGAL STRAIN; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SEQUENCE ALIGNMENT;

AMINO ACID SUBSTITUTION; BINDING SITES; COPPER; CRYPTOCOCCUS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ELECTROSTATICS; ENZYME STABILITY; FUNGAL PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; SUPEROXIDE DISMUTASE;

CRYPTOCOCCUS LIQUEFACIENS;

EID: 48849086512     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.07.046     Document Type: Article

References (26)

1. Iwahashi H., Fujii S., Obuchi K., Kaul S.C., Sato A., and Komatsu Y. Hydrostatic pressure is like high temperature and oxidative stress in the damage it causes to yeast. FEMS Microbiol. Lett. 108 (1993) 53-57
2. Abe F., Kato C., and Horikoshi K. Pressure-regulated metabolism in microorganisms. Trends Microbiol. 7 (1999) 447-453
3. 2+. Biotechnol. Lett. 23 (2001) 2027-2034
4. Minegishi H., Miura T., Yoshida Y., Usami R., and Abe F. Phylogenetic analysis of pectin degrading yeasts from deep-sea environments. J. Jpn. Soc. Extremophiles 5 (2006) 21-26
5. Abe F., Minegishi H., Miura T., Nagahama T., Usami R., and Horikoshi K. Characterization of cold- and high-pressure-active polygalacturonases from a deep-sea yeast, Cryptococcus liquefaciens strain N6. Biosci. Biotechnol. Biochem. 70 (2006) 296-299
6. Miura T., Abe F., Inoue A., Usami R., and Horikoshi K. Superoxide dismutase is involved in high tolerance to copper in the deep-sea yeast, Cryptococcus sp. N6. Biotechnol. Lett. 24 (2002) 1069-1074
7. Fridovich I. The biology of oxygen radicals. Science 201 (1978) 875-880
8. Trush M.A., and Kensler T.W. An overview of the relationship between oxidative stress and chemical carcinogenesis. Free Radic. Biol. Med. 10 (1991) 201-209
9. Fridovich I. Superoxide dismutase. Annu. Rev. Biochem. 44 (1975) 147-159
10. Culotta V.C., Joh H.D., Lin S.J., Slekar K.H., and Strain J. A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering. J. Biol. Chem. 270 (1995) 29991-29997
11. Kanamasa S., Sumi K., Yamuki N., Kumasaka T., Miura T., Abe F., and Kajiwara S. Cloning and functional characterization of the copper/zinc superoxide dismutase gene from the heavy-metal-tolerant yeast Cryptococcus liquefaciens strain N6. Mol. Genet. Genomics 277 (2007) 403-412
12. Culotta V.C., Klomp L.W., Strain J., Casareno R.L., Krems B., and Gitlin J.D. The copper chaperone for superoxide dismutase. J. Biol. Chem. 272 (1997) 23469-23472
13. Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Cryst. 30 (1997) 1022-1025
14. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
15. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53 (1997) 240-255
16. Ramachandran G.N., Ramakrishnan C., and Sasisekharan V. Stereochemistry of polypeptide chain configurations. J. Mol. Biol. 7 (1963) 95-99
17. Chenna R., Sugawara H., Koike T., Lopez R., Gibson T.J., Higgins D.G., and Thompson J.D. Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res. 31 (2003) 3497-3500
18. Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
19. Hart P.J., Balbirnie M.M., Ogihara N.L., Nersissian A.M., Weiss M.S., Valentine J.S., and Eisenberg D. A structure-based mechanism for copper-zinc superoxide dismutase. Biochemistry 38 (1999) 2167-2178
20. Hough M.A., and Hasnain S.S. Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 Å. Structure 11 (2003) 937-946
21. Cardoso R.M., Silva C.H., Ulian de Araújo A.P., Tanaka T., Tanaka M., and Garratt R.C. Structure of the cytosolic Cu,Zn superoxide dismutase from Schistosoma mansoni. Acta Crystallogr. D 60 (2004) 1569-1578
22. Strange R.W., Antonyuk S., Hough M.A., Doucette P.A., Rodriguez J.A., Hart P.J., Hayward L.J., Valentine J.S., and Hasnain S.S. The structure of holo and metal-deficient wild-type human Cu Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis. J. Mol. Biol. 328 (2003) 877-891
23. Ciriolo M.R., Battistoni A., Falconi M., Filomeni G., and Rotilio G. Role of the electrostatic loop of Cu,Zn superoxide dismutase in the copper uptake process. Eur. J. Biochem. 268 (2001) 737-742
24. Lynch S.M., and Colón W. Dominant role of copper in the kinetic stability of Cu/Zn superoxide dismutase. Biochem. Biophys. Res. Commun. 340 (2006) 457-461
25. Matthews B.W., Nicholson H., and Becktel W.J. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. USA 84 (1987) 6663-6667
26. Gåseidnes S., Synstad B., Jia X., Kjellesvik H., Vriend G., and Eijsink V.G. Stabilization of a chitinase from Serratia marcescens by Gly → Ala and Xxx → Pro mutations. Protein Eng. 16 (2003) 841-846