2bhf
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2bhf |SIZE=350|CAPTION= <scene name='initialview01'>2bhf</scene>, resolution 2.50Å | |PDB= 2bhf |SIZE=350|CAPTION= <scene name='initialview01'>2bhf</scene>, resolution 2.50Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene> | + | |LIGAND= <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhf OCA], [http://www.ebi.ac.uk/pdbsum/2bhf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bhf RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Lopes, G G.]] | [[Category: Lopes, G G.]] | ||
[[Category: Martins, L O.]] | [[Category: Martins, L O.]] | ||
| - | [[Category: CU1]] | ||
| - | [[Category: GOL]] | ||
[[Category: laccase]] | [[Category: laccase]] | ||
[[Category: multicopper-oxidase]] | [[Category: multicopper-oxidase]] | ||
| Line 34: | Line 35: | ||
[[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 Mon Mar 31 02:06:27 2008'' |
Revision as of 23:06, 30 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mon Mar 31 02:06:27 2008
