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Titolo:
CRYSTAL-STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM ARTHROBACTER-GLOBIFORMIS IN THE HOLO AND APO FORMS - IMPLICATIONS FOR THE BIOGENESIS OF TOPAQUINONE
Autore:
WILCE MCJ; DOOLEY DM; FREEMAN HC; GUSS JM; MATSUNAMI H; MCINTIRE WS; RUGGIERO CE; TANIZAWA K; YAMAGUCHI H;
Indirizzi:
UNIV SYDNEY,SCH CHEM SYDNEY NSW 2006 AUSTRALIA UNIV SYDNEY,SCH CHEM SYDNEY NSW 2006 AUSTRALIA UNIV SYDNEY,DEPT BIOCHEM SYDNEY NSW 2006 AUSTRALIA MONTANA STATE UNIV,DEPT CHEM & BIOCHEM BOZEMAN MT 59717 DEPT VET AFFAIRS MED CTR,DIV MOL BIOL SAN FRANCISCO CA 94121 UNIV CALIF SAN FRANCISCO,DEPT BIOCHEM & BIOPHYS SAN FRANCISCO CA 94143 UNIV CALIF SAN FRANCISCO,DEPT ANESTHESIA SAN FRANCISCO CA 94143 OSAKA UNIV,INST PROT RES OSAKA 567 JAPAN OSAKA UNIV,INST SCI & IND RES OSAKA 567 JAPAN
Titolo Testata:
Biochemistry
fascicolo: 51, volume: 36, anno: 1997,
pagine: 16116 - 16133
SICI:
0006-2960(1997)36:51<16116:COTCAO>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
TOPA QUINONE COFACTOR; BIOSYNTHESIS; RESOLUTION; OXIDATION; PROGRAM; ERRORS; MAPS;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
M.C.J. Wilce et al., "CRYSTAL-STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM ARTHROBACTER-GLOBIFORMIS IN THE HOLO AND APO FORMS - IMPLICATIONS FOR THE BIOGENESIS OF TOPAQUINONE", Biochemistry, 36(51), 1997, pp. 16116-16133

Abstract

The crystal structures of the copper enzyme phenylethylamine oxidase from the Gram-positive bacterium Arthrobacter globiformis (AGAO) have been determined and refined for three forms of the enzyme: the holoenzyme in its active form (at 2.2 Angstrom resolution), the holoenzyme inan inactive form (at 2.8 Angstrom resolution), and the apoenzyme (at 2.2 Angstrom resolution). The holoenzyme has a topaquinone (TPQ) cofactor formed from the apoenzyme by the post-translational modification of a tyrosine residue in the presence of Cu2+. Significant differences between the three forms of AGAO are limited to the active site. The polypeptide fold is closely similar to those of the amine oxidases from Escherichia coil [Parsons, M. R., et al. (1995) Structure 3, 1171-1184] and pea seedlings [Kumar, V., ct al. (1996) Structure 4, 943-955]. In the active form of holo-AGAO, the active-site Cu atom is coordinatedby three His residues and two water molecules in an approximately square-pyramidal arrangement. In the inactive form, the Cu atom is coordinated by the same three His residues and by the phenolic oxygen of theTPQ, the geometry being quasi-trigonal-pyramidal. There is evidence of disorder in the crystals of both forms of holo-AGAO. As a result, only the position of the aromatic group of the TPQ cofactor, but not itsorientation about the C-beta-C-gamma bond, is determined unequivocally. In apo-AGAO, electron density consistent with an unmodified Tyr occurs at a position close to that of the TPQ in the inactive holo-AGAO. This observation has implications for the biogenesis of TPQ. Two features which have not been described previously in amine oxidase structures are a channel from the molecular surface to the active site and a solvent-filled cavity at the major interface between the two subunits of the dimer.

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Documento generato il 01/12/20 alle ore 08:12:46