3bxv

Crystal structure studies on sulfur oxygenase reductase from Acidianus tengchongensis

spinqualitylabelsall models 3bxv, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3bxv is a 1 chain structure with sequence from Acidianus tengchongensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: FE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q977W3_9CREN 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 Sulfur oxygenase reductase (SOR) simultaneously catalyzes oxidation and reduction of elemental sulfur to produce sulfite, thiosulfate, and sulfide in the presence of molecular oxygen. In this study, crystal structures of wild type and mutants of SOR from Acidianus tengchongensis (SOR-AT) in two different crystal forms were determined and it was observed that 24 identical SOR monomers form a hollow sphere. Within the icosatetramer sphere, the tetramer and trimer channels were proposed as the paths for the substrate and products, respectively. Moreover, a comparison of SOR-AT with SOR-AA (SOR from Acidianus ambivalens) structures showed that significant differences existed at the active site. Firstly, Cys31 is not persulfurated in SOR-AT structures. Secondly, the iron atom is five-coordinated rather than six-coordinated, since one of the water molecules ligated to the iron atom in the SOR-AA structure is lost. Consequently, the binding sites of substrates and a hypothetical catalytic process of SOR were proposed. Crystal structure studies on sulfur oxygenase reductase from Acidianus tengchongensis.,Li M, Chen Z, Zhang P, Pan X, Jiang C, An X, Liu S, Chang W Biochem Biophys Res Commun. 2008 May 9;369(3):919-23. Epub 2008 Mar 7. PMID:18329378 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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