1rie
From Proteopedia
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STRUCTURE OF A WATER SOLUBLE FRAGMENT OF THE RIESKE IRON-SULFUR PROTEIN OF THE BOVINE HEART MITOCHONDRIAL CYTOCHROME BC1-COMPLEX
Overview
BACKGROUND: The 'Rieske' iron-sulfur protein is the primary electron, acceptor during hydroquinone oxidation in cytochrome bc complexes. The, spectroscopic and electrochemical properties of the 'Rieske' [2Fe-2S], cluster differ significantly from those of other iron-sulfur clusters. A, 129-residue water soluble fragment containing the intact [2Fe-2S] cluster, was isolated following proteolytic digestion of the bc1 complex and used, for structural studies. RESULTS: The structure of the Rieske iron-sulfur, fragment containing the reduced [2Fe-2S] cluster has been determined using, the multiwavelength anomalous diffraction (MAD) technique and refined at, 1.5 A resolution. The fragment has a novel overall fold that includes, three sheets of beta strands. The iron atoms of the [2Fe-2S] cluster ... [(full description)]
About this Structure
1RIE is a [Single protein] structure of sequence from [Bos taurus] with FES as [ligand]. Active as [Ubiquinol--cytochrome-c reductase], with EC number [1.10.2.2]. Structure known Active Site: IRO. Full crystallographic information is available from [OCA].
Reference
Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution., Iwata S, Saynovits M, Link TA, Michel H, Structure. 1996 May 15;4(5):567-79. PMID:8736555
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