Crystal structures of Pseudomonas syringae pv. tomato DC3000 quinone oxidoreductase and its complex with NADPH

Biochemical and Biophysical Research Communications

Volumn 390, Issue 3, 2009, Pages 597-602

  Pan, Xiaowei ^a,b   Zhang, Hongmei ^a   Gao, Yu ^a   Li, Mei ^a   Chang, Wenrui ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

Conformational change; Crystal structure; NADPH; Quinone oxidoreductase; Zeta crystallin

Indexed keywords

DIMER; GENOMIC DNA; OXIDOREDUCTASE; PHENANTHRENEQUINONE; QUINONE OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SEMIQUINONE; UNCLASSIFIED DRUG; ZETA CRYSTALLIN;

ANIMAL CELL; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE EXPRESSION; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PSEUDOMONAS SYRINGAE; THERMUS THERMOPHILUS;

BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY; ESCHERICHIA COLI; NAD(P)H DEHYDROGENASE (QUINONE); NADP; PROTEIN CONFORMATION; PSEUDOMONAS SYRINGAE; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; PSEUDOMONAS SYRINGAE PV. TOMATO; THERMUS THERMOPHILUS;

EID: 70449724582     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.10.012     Document Type: Article

References (25)

1. Kim I.K., Yim H.S., Kim M.K., Kim D.W., Kim Y.M., Cha S.S., and Kang S.O. Crystal structure of a new type of NADPH-dependent quinone oxidoreductase (QOR2) from Escherichia coli. J. Mol. Biol. 379 (2008) 372-384
2. Yagi T. Bacterial NADH-quinone oxidoreductases. J. Bioenerg. Biomembr. 23 (1991) 211-225
3. Duhaiman A.S., Rabbani N., AlJafari A.A., and Alhomida A.S. Purification and characterization of zeta-crystallin from the camel lens. Biochem. Biophys. Res. Commun. 215 (1995) 632-640
4. Gonzalez P., Rao P.V., and Zigler Jr. J.S. Molecular cloning and sequencing of zeta-crystallin/quinone reductase cDNA from human liver. Biochem. Biophys. Res. Commun. 191 (1993) 902-907
5. Rao P.V., and Zigler J.S. Crystallin from guinea pig lens is capable of functioning catalytically as an oxidoreductase. Arch. Biochem. Biophys. 167 (1991) 1221-1228
6. Rao P.V., and Zigler J.S. Purification and characterization of zetacrystallin/quinone reductase from guinea pig live. Biochim. Biophys. Acta 1117 (1992) 315-320
7. Rodokanaki A., Holmes R.K., and Borra's T. Zeta-crystallin, a novel protein from guinea pig lens is related to alcohol dehydrogenases. Gene 78 (1989) 215-224
8. Rao P.V., Krishna C.M., and Zigler J.S. Identification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. J. Biol. Chem. 267 (1992) 96-102
9. Rao S.T., and Rossmann M.G. Comparison of super-secondary structures in proteins. J. Mol. Biol. 76 (1973) 241-256
10. Mano J., Torii Y., Hayashi S., Takimoto K., Matsui K., Nakamura K., Inze D., Babiychuk E., Kushnir S., and Asada K. The NADPH:quinone oxidoreductase P1-zeta-crystallin in Arabidopsis catalyzes the alpha, beta-hydrogenation of 2-alkenals: detoxication of the lipid peroxide-derived reactive aldehydes. Plant Cell Physiol. 43 (2002) 1445-1455
11. Mano J., Yoon H., Asada K., Babiychuk E., Inze D., and Mikami B. Crystallization and preliminary X-ray crystallographic analysis of NADPH:azodicarbonyl/quinone oxidoreductase, a plant zeta-crystallin. Biochim. Biophys. Acta 1480 (2000) 374-376
12. Mano J., Babiychuk E., Belles-Boix E., Hiratake J., Kimura A., Inze D., Kushnir S., and Asada K. A novel NADPH:diamide oxidoreductase activity in Arabidopsis thaliana P1 zeta-crystallin. Eur. J. Biochem. 267 (2000) 3661-3671
13. Tumminia S.J., Rao P.V., Zigler Jr. J.S., and Russell P. Xenobiotic induction of quinone oxidoreductase activity in lens epithelial cells. Biochim. Biophys. Acta 1203 (1993) 251-259
14. Thorn J.M., Barton J.D., Dixon N.E., Ollis D.L., and Edwards K.J. Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH. J. Mol. Biol. 249 (1995) 785-799
15. Shimomura Y., Kakuta Y., and Fukuyama K. Crystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: implication for NADPH and substrate recognition. J. Bacteriol. 185 (2003) 4211-4218
16. Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T., Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R., Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B., Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., and Collmer A. The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000. Proc. Natl. Acad. Sci. USA 100 (2003) 10181-10186
17. Minor Z.O.a.W. Processing of X-ray diffraction data collected in oscillation mode. Methods in enzymology. Macromol. Crystallogr. A 276 (1997) 307-326
18. McCoy A.J., Grosse-Kunstleve R.W., Adams P.D., Winn M.D., Storoni L.C., and Read R.J. Phaser crystallographic software. J. Appl. Crystallogr. 40 (2007) 658-674
19. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763.
20. Zwart P.H., Afonine P.V., Grosse-Kunstleve R.W., Hung L.W., Ioerger T.R., McCoy A.J., McKee E., Moriarty N.W., Read R.J., Sacchettini J.C., Sauter N.K., Storoni L.C., Terwilliger T.C., and Adams P.D. Automated structure solution with the PHENIX suite. Methods Mol. Biol. 426 (2008) 419-435
21. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53 (1997) 240-255
22. 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 Biol. Crystallogr. 54 (1998) 905-921
23. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 2126-2132
24. 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. Cryst. 26 (1993) 283-291
25. Krissinel E., and Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 2256-2268