1do6

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[[Image:1do6.gif|left|200px]]
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{{STRUCTURE_1do6| PDB=1do6 | SCENE= }}
{{STRUCTURE_1do6| PDB=1do6 | SCENE= }}
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'''CRYSTAL STRUCTURE OF SUPEROXIDE REDUCTASE IN THE OXIDIZED STATE AT 2.0 ANGSTROM RESOLUTION'''
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===CRYSTAL STRUCTURE OF SUPEROXIDE REDUCTASE IN THE OXIDIZED STATE AT 2.0 ANGSTROM RESOLUTION===
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==Overview==
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Superoxide reductase (SOR) is a blue non-heme iron protein that functions in anaerobic microbes as a defense mechanism against reactive oxygen species by catalyzing the reduction of superoxide to hydrogen peroxide [Jenney, F. E., Jr., Verhagen, M. F. J. M., Cui, X. , and Adams, M. W. W. (1999) Science 286, 306-309]. Crystal structures of SOR from the hyperthermophilic archaeon Pyrococcus furiosus have been determined in the oxidized and reduced forms to resolutions of 1.7 and 2.0 A, respectively. SOR forms a homotetramer, with each subunit adopting an immunoglobulin-like beta-barrel fold that coordinates a mononuclear, non-heme iron center. The protein fold and metal center are similar to those observed previously for the homologous protein desulfoferrodoxin from Desulfovibrio desulfuricans [Coelho, A. V., Matias, P., Fulop, V., Thompson, A., Gonzalez, A., and Carrondo, M. A. (1997) J. Bioinorg. Chem. 2, 680-689]. Each iron is coordinated to imidazole nitrogens of four histidines in a planar arrangement, with a cysteine ligand occupying an axial position normal to this plane. In two of the subunits of the oxidized structure, a glutamate carboxylate serves as the sixth ligand to form an overall six-coordinate, octahedral coordinate environment. In the remaining two subunits, the sixth coordination site is either vacant or occupied by solvent molecules. The iron centers in all four subunits of the reduced structure exhibit pentacoordination. The structures of the oxidized and reduced forms of SOR suggest a mechanism by which superoxide accessibility may be controlled and define a possible binding site for rubredoxin, the likely physiological electron donor to SOR.
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(as it appears on PubMed at http://www.pubmed.gov), where 10704199 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10704199}}
==About this Structure==
==About this Structure==
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[[Category: Yeh, A P.]]
[[Category: Yeh, A P.]]
[[Category: Non-heme iron protein]]
[[Category: Non-heme iron protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:04:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:21:59 2008''

Revision as of 20:22, 30 June 2008

Image:1do6.png

Template:STRUCTURE 1do6

CRYSTAL STRUCTURE OF SUPEROXIDE REDUCTASE IN THE OXIDIZED STATE AT 2.0 ANGSTROM RESOLUTION

Template:ABSTRACT PUBMED 10704199

About this Structure

1DO6 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

Reference

Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states., Yeh AP, Hu Y, Jenney FE Jr, Adams MW, Rees DC, Biochemistry. 2000 Mar 14;39(10):2499-508. PMID:10704199

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