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1OA0

REDUCED HYBRID CLUSTER PROTEIN FROM DESULFOVIBRIO DESULFURICANS X-RAY STRUCTURE AT 1.25A RESOLUTION

Summary for 1OA0
Entry DOI10.2210/pdb1oa0/pdb
Related1GN9 1GNL 1OA1
DescriptorPRISMANE PROTEIN, IRON/SULFUR CLUSTER, FE4-S3 CLUSTER, ... (5 entities in total)
Functional Keywordshybrid cluster protein, hybrid cluster, desulfovibrio desulfuricans, reduced forms, high-resolution
Biological sourceDESULFOVIBRIO DESULFURICANS
Total number of polymer chains2
Total formula weight118729.42
Authors
Primary citationAragao, 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.
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., 8:540-548, 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: 12764602
DOI: 10.1007/s00775-003-0443-x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.25 Å)
Structure validation

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数据于2025-06-25公开中

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