2v4j

THE CRYSTAL STRUCTURE OF Desulfovibrio vulgaris DISSIMILATORY SULFITE REDUCTASE BOUND TO DsrC PROVIDES NOVEL INSIGHTS INTO THE MECHANISM OF SULFATE RESPIRATION

spinqualitylabelsall models 2v4j, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2v4j is a 6 chain structure with sequence from Desulfovibrio vulgaris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SF4, SH0, SO3, SRM Activity: Hydrogensulfite reductase, with EC number 1.8.99.3 Resources: FirstGlance, OCA, RCSB, PDBsum Function [DSVA_DESVH] Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration, a process catalyzed by the sulfate-reducing bacteria. [DSVB_DESVH] Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration, a process catalyzed by the sulfate-reducing bacteria. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Sulfate reduction is one of the earliest types of energy metabolism used by ancestral organisms to sustain life. Despite extensive studies, many questions remain about the way respiratory sulfate reduction is associated with energy conservation. A crucial enzyme in this process is the dissimilatory sulfite reductase (dSiR), which contains a unique siroheme-[4Fe4S] coupled cofactor. Here, we report the structure of desulfoviridin from Desulfovibrio vulgaris, in which the dSiR DsrAB (sulfite reductase) subunits are bound to the DsrC protein. The alpha(2)beta(2)gamma(2) assembly contains two siroheme-[4Fe4S] cofactors bound by DsrB, two sirohydrochlorins and two [4Fe4S] centers bound by DsrA, and another four [4Fe4S] centers in the ferredoxin domains. A sulfite molecule, coordinating the siroheme, is found at the active site. The DsrC protein is bound in a cleft between DsrA and DsrB with its conserved C-terminal cysteine reaching the distal side of the siroheme. We propose a novel mechanism for the process of sulfite reduction involving DsrAB, DsrC, and the DsrMKJOP membrane complex (a membrane complex with putative disulfide/thiol reductase activity), in which two of the six electrons for reduction of sulfite derive from the membrane quinone pool. These results show that DsrC is involved in sulfite reduction, which changes the mechanism of sulfate respiration. This has important implications for models used to date ancient sulfur metabolism based on sulfur isotope fractionations. The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration.,Oliveira TF, Vonrhein C, Matias PM, Venceslau SS, Pereira IA, Archer M J Biol Chem. 2008 Dec 5;283(49):34141-9. Epub 2008 Sep 30. PMID:18829451 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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