1OAC

CRYSTAL STRUCTURE OF A QUINOENZYME: COPPER AMINE OXIDASE OF ESCHERICHIA COLI AT 2 ANGSTROEMS RESOLUTION

Summary for 1OAC

• Entry DOI: 10.2210/pdb1oac/pdb
• Descriptor: COPPER AMINE OXIDASE, COPPER (II) ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase, copper, tpq, periplasmic
• Biological source: Escherichia coli
• Cellular location: Periplasm: P46883
• Total number of polymer chains: 2
• Total formula weight: 163020.86

Authors

Parsons, M.R.,Convery, M.A.,Wilmot, C.M.,Phillips, S.E.V. (deposition date: 1995-09-27, release date: 1996-04-03, Last modification date: 2011-07-13)

Primary citation

Parsons, M.R.,Convery, M.A.,Wilmot, C.M.,Yadav, K.D.,Blakeley, V.,Corner, A.S.,Phillips, S.E.,McPherson, M.J.,Knowles, P.F.
Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.
Structure, 3:1171-1184, 1995

PubMed Abstract: Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).

PubMed: 8591028
DOI: 10.1016/S0969-2126(01)00253-2

Experimental method

X-RAY DIFFRACTION (2 Å)