2X88

Crystal Structure of HoloCotA

Summary for 2X88

• Entry DOI: 10.2210/pdb2x88/pdb
• Related: 1GSK 1OF0 1UVW 1W6L 1W6W 1W8E 2BHF 2X87
• Descriptor: SPORE COAT PROTEIN A, COPPER (II) ION, OXYGEN MOLECULE, ... (5 entities in total)
• Functional Keywords: oxidoreductase, oxidase, laccase, sporulation, oxygen reduction, multicopper-oxidase
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 1
• Total formula weight: 59279.04

Authors

Bento, I.,Silva, C.S.,Chen, Z.,Martins, L.O.,Lindley, P.F.,Soares, C.M. (deposition date: 2010-03-06, release date: 2010-09-22, Last modification date: 2024-11-13)

Primary citation

Bento, I.,Silva, C.S.,Chen, Z.,Martins, L.O.,Lindley, P.F.,Soares, C.M.
Mechanisms Underlying Dioxygen Reduction in Laccases. Structural and Modelling Studies Focusing on Proton Transfer.
Bmc Struct.Biol., 10:29-, 2010

PubMed Abstract: Laccases are enzymes that couple the oxidation of substrates with the reduction of dioxygen to water. They are the simplest members of the multi-copper oxidases and contain at least two types of copper centres; a mononuclear T1 and a trinuclear that includes two T3 and one T2 copper ions. Substrate oxidation takes place at the mononuclear centre whereas reduction of oxygen to water occurs at the trinuclear centre.

PubMed: 20822511
DOI: 10.1186/1472-6807-10-28

Experimental method

X-RAY DIFFRACTION (1.8 Å)