This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1rie
From Proteopedia
|
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
Page seeded by OCA on Tue Oct 30 16:03:24 2007
