1b4n

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Revision as of 21:35, 24 November 2007

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spinqualitylabelsall models 1b4n, resolution 2.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM PYROCOCCUS FURIOSUS, COMPLEXED WITH GLUTARATE

Overview

Crystal structures of formaldehyde ferredoxin oxidoreductase (FOR), a, tungstopterin-containing protein from the hyperthermophilic archaeon, Pyrococcus furiosus, have been determined in the native state and as a, complex with the inhibitor glutarate at 1.85 A and 2. 4 A resolution, respectively. The native structure was solved by molecular replacement, using the structure of the homologous P. furiosus aldehyde ferredoxin, oxidoreductase (AOR) as the initial model. Residues are identified in FOR, that may be involved in either the catalytic mechanism or in determining, substrate specificity. The binding site on FOR for the physiological, electron acceptor, P. furiosus ferredoxin (Fd), has been established from, an FOR-Fd cocrystal structure. Based on the arrangement of redox centers, in this structure, an electron transfer pathway is proposed that begins at, the tungsten center, leads to the (4Fe:4S) cluster of FOR via one of the, two pterins that coordinate the tungsten, and ends at the (4Fe:4S) cluster, of ferredoxin. This pathway includes two residues that coordinate the, (4Fe:4S) clusters, Cys287 of FOR and Asp14 of ferredoxin. Similarities in, the active site structures between FOR and the unrelated molybdoenzyme, aldehyde oxidoreductase from Desulfovibrio gigas suggest that both enzymes, utilize a common mechanism for aldehyde oxidation.

About this Structure

1B4N is a Single protein structure of sequence from Pyrococcus furiosus with CA, SF4, GUA and PTE as ligands. Full crystallographic information is available from OCA.

Reference

Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 A resolution crystal structure and its mechanistic implications., Hu Y, Faham S, Roy R, Adams MW, Rees DC, J Mol Biol. 1999 Feb 26;286(3):899-914. PMID:10024458

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