4dmr

From Proteopedia

Revision as of 15:42, 30 October 2007

REDUCED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS WITH BOUND DMSO SUBSTRATE

Overview

The crystal structure of the molybdenum enzyme dimethylsulphoxide, reductase (DMSOR) has been determined at 1.9 A resolution with substrate, bound at the active site. DMSOR is an oxotransferase which catalyses the, reduction of dimethylsulphoxide (DMSO) to dimethylsulphide (DMS) in a two, stage reaction which is linked to oxygen atom transfer and electron, transfer. In the first step, DMSO binds to reduced (Mo(IV)) enzyme, the, enzyme is oxidised to Mo(VI) with an extra oxygen ligand and DMS is, released. Regeneration of reduced enzyme is achieved by transfer of two, electrons, successively from a specific cytochrome, and release of the, oxygen as water. The enzyme, purified under aerobic conditions, is in the, oxidised (Mo(VI)) state. Addition of a large excess of DMS to the oxidised, ... [(full description)]

About this Structure

4DMR is a [Single protein] structure of sequence from [Rhodobacter capsulatus] with PGD, 4MO, O and DMS as [ligands]. Structure known Active Site: MO. Full crystallographic information is available from [OCA].

Reference

The high resolution crystal structure of DMSO reductase in complex with DMSO., McAlpine AS, McEwan AG, Bailey S, J Mol Biol. 1998 Jan 30;275(4):613-23. PMID:9466935

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