1dxg
From Proteopedia
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CRYSTAL STRUCTURE OF DESULFOREDOXIN FROM DESULFOVIBRIO GIGAS AT 1.8 A RESOLUTION
Overview
The crystal structure of desulforedoxin from Desulfovibrio gigas, a new, homo-dimeric (2 x 36 amino acids) non-heme iron protein, has been solved, by the SIRAS method using the indium-substituted protein as the single, derivative. The structure was refined to a crystallographic R-factor of, 16.9% at 1.8 A resolution. Native desulforedoxin crystals were grown from, either PEG 4K or lithium sulfate, with cell constants a = b = 42.18 A, c =, 72.22 A (for crystals grown from PEG 4K), and they belong to space group, P3(2)21. The indium-substituted protein crystallized isomorphously under, the same conditions. The 2-fold symmetric dimer is firmly hydrogen bonded, and folds as an incomplete beta-barrel with the two iron centers placed on, opposite poles of the molecule. Each iron atom is coordinated to four, cysteinyl residues in a distorted tetrahedral arrangement. Both iron atoms, are 16 A apart but connected across the 2-fold axis by 14 covalent bonds, along the polypeptide chain plus two hydrogen bonds. Desulforedoxin and, rubredoxin share some structural features but show significant differences, in terms of metal environment and water structure, which account for the, known spectroscopic differences between rubredoxin and desulforedoxin.
About this Structure
1DXG is a Single protein structure of sequence from Desulfovibrio gigas with FE as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 A resolution: a novel non-heme iron protein structure., Archer M, Huber R, Tavares P, Moura I, Moura JJ, Carrondo MA, Sieker LC, LeGall J, Romao MJ, J Mol Biol. 1995 Sep 1;251(5):690-702. PMID:7666420
Page seeded by OCA on Tue Nov 20 13:39:37 2007
