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1w6l
From Proteopedia
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3D STRUCTURE OF COTA INCUBATED WITH CUCL2
Overview
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, ... [(full description)]
About this Structure
1W6L is a [Single protein] structure of sequence from [Bacillus subtilis] with CU, OXY and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Tue Oct 30 13:50:41 2007
Categories: Bacillus subtilis | Single protein | Bento, I. | Carrondo, M.A. | Lindley, P.F. | Lopes, G.G. | Martins, L.O. | CU | GOL | OXY | Copper | Laccase | Multicopper-oxidase | Oxidase | Oxygen reduction
