1oac

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

File:1oac.jpg


1oac, resolution 2.0Å

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OverviewOverview

BACKGROUND: 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). RESULTS: The, crystal structure of amine oxidase from Escherichia coli has been, determined in both an active and an inactive form. The only structural, differences are in the active site, where differences in copper, coordination geometry and in the position and interactions of the redox, cofactor, TPQ, are observed. Each subunit of the mushroom-shaped dimer, comprises four domains: a 440 amino acid C-terminal beta sandwich domain, which contains the active site and provides the dimer interface, and three, smaller peripheral alpha/beta domains (D1-D3), each of about 100 amino, acids. D2 and D3 show remarkable structural and sequence similarity to, each other and are conserved throughout the quinoenzyme family. In, contrast, D1 is absent from some amine oxidases. The active sites are well, buried from solvent and lie some 35 A apart, connected by a pair of beta, hairpin arms. CONCLUSIONS: The crystal structure of E. coli copper amine, oxidase reveals a number of unexpected features and provides a basis for, investigating the intriguing similarities and differences in catalytic, mechanism of members of this enzyme family. In addition to the three, conserved histidines that bind the copper, our studies identify a number, of other conserved residues close to the active site, including a, candidate for the catalytic base and a fourth conserved histidine which is, involved in an interesting intersubunit interaction.

About this StructureAbout this Structure

1OAC is a Single protein structure of sequence from Escherichia coli with CU and CA as ligands. Active as Amine oxidase (copper-containing), with EC number 1.4.3.6 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution., Parsons MR, Convery MA, Wilmot CM, Yadav KD, Blakeley V, Corner AS, Phillips SE, McPherson MJ, Knowles PF, Structure. 1995 Nov 15;3(11):1171-84. PMID:8591028

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