4pw3

Crystal structure of the sulfite dehydrogenase SorT from Sinorhizobium meliloti

spinqualitylabelsall models 4pw3, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pw3 is a 4 chain structure with sequence from Ensifer meliloti. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, MSS Related: 4pw9, 4pwa Gene: R02832, SMc04049 (Ensifer meliloti) Activity: Sulfite oxidase, with EC number 1.8.3.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q92M24_RHIME] The exact function is not known. Can catalyze the reduction of a variety of substrates like dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide. Cannot reduce cyclic N-oxides. Shows no activity as sulfite oxidase.[SAAS:SAAS00086612] Publication Abstract from PubMed Interprotein electron transfer underpins the essential processes of life and relies on the formation of specific, yet transient protein-protein interactions. In biological systems, the detoxification of sulfite is catalyzed by the sulfite-oxidizing enzymes (SOEs), which interact with an electron acceptor for catalytic turnover. Here, we report the structural and functional analyses of the SOE SorT from Sinorhizobium meliloti and its cognate electron acceptor SorU. Kinetic and thermodynamic analyses of the SorT/SorU interaction show the complex is dynamic in solution, and that the proteins interact with Kd = 13.5 +/- 0.8 muM. The crystal structures of the oxidized SorT and SorU, both in isolation and in complex, reveal the interface to be remarkably electrostatic, with an unusually large number of direct hydrogen bonding interactions. The assembly of the complex is accompanied by an adjustment in the structure of SorU, and conformational sampling provides a mechanism for dissociation of the SorT/SorU assembly. Structural basis of interprotein electron transfer in bacterial sulfite oxidation.,McGrath AP, Laming EL, Casas Garcia GP, Kvansakul M, Guss JM, Trewhella J, Calmes B, Bernhardt PV, Hanson GR, Kappler U, Maher MJ Elife. 2015 Dec 19;4. pii: e09066. doi: 10.7554/eLife.09066. PMID:26687009 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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