1d4d
From Proteopedia
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CRYSTAL STRUCTURE OF THE SUCCINATE COMPLEXED FORM OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1
Overview
Fumarate respiration is one of the most widespread types of anaerobic, respiration. The soluble fumarate reductase of Shewanella putrefaciens, MR-1 is a periplasmic tetraheme flavocytochrome c. The crystal structures, of the enzyme were solved to 2.9 A for the uncomplexed form and to 2.8 A, and 2.5 A for the fumarate and the succinate-bound protein, respectively., The structures reveal a flexible capping domain linked to the FAD-binding, domain. A catalytic mechanism for fumarate reduction based on the, structure of the complexed protein is proposed. The mechanism for the, reverse reaction is a model for the homologous succinate dehydrogenase, (complex II) of the respiratory chain. In flavocytochrome c fumarate, reductase, all redox centers are in van der Waals contact with one, another, thus providing an efficient conduit of electrons from the hemes, via the FAD to fumarate.
About this Structure
1D4D is a Single protein structure of sequence from Shewanella putrefaciens with HEM, FAD and SIN as ligands. Active as Succinate dehydrogenase, with EC number 1.3.99.1 Full crystallographic information is available from OCA.
Reference
Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1., Leys D, Tsapin AS, Nealson KH, Meyer TE, Cusanovich MA, Van Beeumen JJ, Nat Struct Biol. 1999 Dec;6(12):1113-7. PMID:10581551
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