1R0I
cadmium-substituted rubredoxin
Summary for 1R0I
Entry DOI | 10.2210/pdb1r0i/pdb |
Related | 1R0F 1R0G 1R0H 1R0J |
Descriptor | Rubredoxin, CADMIUM ION (3 entities in total) |
Functional Keywords | rubredoxin, iron-sulfur, clostridium pasteurianum, electron transport |
Biological source | Clostridium pasteurianum |
Total number of polymer chains | 1 |
Total formula weight | 6164.02 |
Authors | Maher, M.,Cross, M.,Wilce, M.C.J.,Guss, J.M.,Wedd, A.G. (deposition date: 2003-09-22, release date: 2004-02-10, Last modification date: 2023-10-25) |
Primary citation | Maher, M.,Cross, M.,Wilce, M.C.,Guss, J.M.,Wedd, A.G. Metal-substituted derivatives of the rubredoxin from Clostridium pasteurianum. Acta Crystallogr.,Sect.D, 60:298-303, 2004 Cited by PubMed Abstract: 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. PubMed: 14747706DOI: 10.1107/S090744490302794X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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