Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1OA1

REDUCED HYBRID CLUSTER PROTEIN (HCP) FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH STRUCTURE AT 1.55A RESOLUTION USING SYNCHROTRON RADIATION.

Summary for 1OA1
Entry DOI10.2210/pdb1oa1/pdb
Related1E1D 1E2U 1E9V 1GNT 1OA0
DescriptorHYDROXYLAMINE REDUCTASE, IRON/SULFUR CLUSTER, FE4-S3 CLUSTER, ... (5 entities in total)
Functional Keywordsoxidoreductase, reduced forms
Biological sourceDESULFOVIBRIO VULGARIS
Total number of polymer chains1
Total formula weight60898.04
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.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: 12764602
DOI: 10.1007/S00775-003-0443-X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon