1r0h
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cobalt-substituted rubredoxin
OverviewOverview
Five different metal-substituted forms of Clostridium pasteurianum, rubredoxin have been prepared and crystallized. The single Fe atom present, in the Fe(S-Cys)(4) site of the native form of the protein was exchanged, in turn for Co, Ni, Ga, Cd and Hg. All five forms of rubredoxin, crystallized in space group R3 and were isomorphous with the native, protein. The Co-, Ni- and Ga-substituted proteins exhibited metal sites, with geometries similar to that of the Fe form (effective D(2d) local, symmetry), as did the Cd and Hg proteins, but with a significant expansion, of the metal-sulfur bond lengths. A knowledge of these structures, contributes to a molecular understanding of the function of this simple, iron-sulfur electron-transport protein.
About this StructureAbout this Structure
1R0H is a Single protein structure of sequence from Clostridium pasteurianum with CO as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Metal-substituted derivatives of the rubredoxin from Clostridium pasteurianum., Maher M, Cross M, Wilce MC, Guss JM, Wedd AG, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):298-303. Epub 2004, Jan 23. PMID:14747706
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