1vzi
From Proteopedia
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|PDB= 1vzi |SIZE=350|CAPTION= <scene name='initialview01'>1vzi</scene>, resolution 1.15Å | |PDB= 1vzi |SIZE=350|CAPTION= <scene name='initialview01'>1vzi</scene>, resolution 1.15Å | ||
|SITE= <scene name='pdbsite=AC1:Fe2+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Fe2+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Superoxide_reductase Superoxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.2 1.15.1.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_reductase Superoxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.2 1.15.1.2] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzi OCA], [http://www.ebi.ac.uk/pdbsum/1vzi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vzi RCSB]</span> | ||
}} | }} | ||
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[[Category: Niviere, V.]] | [[Category: Niviere, V.]] | ||
[[Category: Royant, A.]] | [[Category: Royant, A.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: FE2]] | ||
[[Category: dinuclear iron cluster]] | [[Category: dinuclear iron cluster]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
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[[Category: redox state]] | [[Category: redox state]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:29:05 2008'' |
Revision as of 21:29, 30 March 2008
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| , resolution 1.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Superoxide reductase, with EC number 1.15.1.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF SUPEROXIDE REDUCTASE BOUND TO FERROCYANIDE AND ACTIVE SITE EXPANSION UPON X-RAY INDUCED PHOTOREDUCTION
Overview
Some sulfate-reducing and microaerophilic bacteria rely on the enzyme superoxide reductase (SOR) to eliminate the toxic superoxide anion radical (O2*-). SOR catalyses the one-electron reduction of O2*- to hydrogen peroxide at a nonheme ferrous iron center. The structures of Desulfoarculus baarsii SOR (mutant E47A) alone and in complex with ferrocyanide were solved to 1.15 and 1.7 A resolution, respectively. The latter structure, the first ever reported of a complex between ferrocyanide and a protein, reveals that this organo-metallic compound entirely plugs the SOR active site, coordinating the active iron through a bent cyano bridge. The subtle structural differences between the mixed-valence and the fully reduced SOR-ferrocyanide adducts were investigated by taking advantage of the photoelectrons induced by X-rays. The results reveal that photo-reduction from Fe(III) to Fe(II) of the iron center, a very rapid process under a powerful synchrotron beam, induces an expansion of the SOR active site.
About this Structure
1VZI is a Single protein structure of sequence from Desulfovibrio baarsii. Full crystallographic information is available from OCA.
Reference
Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction., Adam V, Royant A, Niviere V, Molina-Heredia FP, Bourgeois D, Structure. 2004 Sep;12(9):1729-40. PMID:15341736
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