1w8e

3D structure of CotA incubated with hydrogen peroxide

spinqualitylabelsall models 1w8e, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1w8e is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CU, GOL, PER Related: 1gsk, 1hkp, 1hkz, 1hl0, 1hl1, 1of0, 1ogr, 1uvw, 1w6l, 1w6w, 2bhf Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [COTA_BACSU] Involved in brown pigmentation during sporogenesis. 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 The multi-copper oxidases oxidise substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water. The precise mechanism of this reduction has been unclear, but recent X-ray structural studies using the CotA endospore coat protein from Bacillus subtilis have given further insights into the principal stages. It is proposed that the mechanism involves binding of the dioxygen into the trinuclear centre so that it is sited approximately symmetrically between the two type 3 copper ions with one oxygen atom close to the type 2 copper ion. Further stages involve the formation of a peroxide intermediate and following the splitting of this intermediate, the migration of the hydroxide moieties towards the solvent exit channel. The migration steps are likely to involve a movement of the type 2 copper ion and its environment. Details of a putative mechanism are described herein based both on structures already reported in the literature and on structures of the CotA protein in the oxidised and reduced states and with the addition of peroxide and the inhibitor, azide. Dioxygen reduction by multi-copper oxidases; a structural perspective.,Bento I, Martins LO, Gato Lopes G, Armenia Carrondo M, Lindley PF Dalton Trans. 2005 Nov 7;(21):3507-13. Epub 2005 Sep 27. PMID:16234932 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CotA laccase

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