1OA1
REDUCED HYBRID CLUSTER PROTEIN (HCP) FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH STRUCTURE AT 1.55A RESOLUTION USING SYNCHROTRON RADIATION.
Summary for 1OA1
Entry DOI | 10.2210/pdb1oa1/pdb |
Related | 1E1D 1E2U 1E9V 1GNT 1OA0 |
Descriptor | HYDROXYLAMINE REDUCTASE, IRON/SULFUR CLUSTER, FE4-S3 CLUSTER, ... (5 entities in total) |
Functional Keywords | oxidoreductase, reduced forms |
Biological source | DESULFOVIBRIO VULGARIS |
Total number of polymer chains | 1 |
Total formula weight | 60898.04 |
Authors | Aragao, D.,Macedo, S.,Mitchell, E.P.,Romao, C.V.,Liu, M.Y.,Frazao, C.,Saraiva, L.M.,Xavier, A.V.,Legall, J.,Van Dongen, W.M.A.M.,Hagen, W.R.,Teixeira, M.,Carrondo, M.A.,Lindley, P.F. (deposition date: 2002-12-23, release date: 2003-04-08, Last modification date: 2024-05-01) |
Primary citation | Aragao, D.,Macedo, S.,Mitchell, E.P.,Romao, C.V.,Liu, M.Y.,Frazao, C.,Saraiva, L.M.,Xavier, A.V.,Legall, J.,Van Dongen, W.M.A.M.,Hagen, W.R.,Teixeira, M.,Carrondo, M.A.,Lindley, P.F. Reduced Hybrid Cluster Proteins (Hcp) from Desulfovibrio Desulfuricans Atcc 27774 and Desulfovibrio Vulgaris (Hildenborough): X-Ray Structures at High Resolution Using Synchrotron Radiation J.Biol.Inorg.Chem., 8:540-, 2003 Cited by PubMed Abstract: The hybrid cluster proteins from the sulfate reducing bacteria Desulfovibrio desulfuricans ATCC 27774 ( Dd) and Desulfovibrio vulgaris strain Hildenborough ( Dv) have been isolated and crystallized anaerobically. In each case, the protein has been reduced with dithionite and the crystal structure of the reduced form elucidated using X-ray synchrotron radiation techniques at 1.25 A and 1.55 A resolution for Dd and Dv, respectively. Although the overall structures of the proteins are unchanged upon reduction, there are significant changes at the hybrid cluster centres. These include significant movements in the position of the iron atom linked to the persulfide moiety in the oxidized as-isolated proteins and the sulfur atom of the persulfide itself. The nature of these changes is described and the implications with respect to the function of hybrid cluster proteins are discussed. PubMed: 12764602DOI: 10.1007/S00775-003-0443-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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