2bhf
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The multi-copper oxidases oxidise substrate molecules by accepting | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bento, I.]] | [[Category: Bento, I.]] | ||
| - | [[Category: Carrondo, M | + | [[Category: Carrondo, M A.]] |
| - | [[Category: Lindley, P | + | [[Category: Lindley, P F.]] |
| - | [[Category: Lopes, G | + | [[Category: Lopes, G G.]] |
| - | [[Category: Martins, L | + | [[Category: Martins, L O.]] |
[[Category: CU1]] | [[Category: CU1]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: oxygen reduction]] | [[Category: oxygen reduction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:58 2008'' |
Revision as of 14:37, 21 February 2008
|
3D STRUCTURE OF THE REDUCED FORM OF COTA
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 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.
About this Structure
2BHF is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Known structural/functional Site: . 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
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