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Titolo:
Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 angstrom and 2.03 angstrom
Autore:
Ellis, PJ; Conrads, T; Hille, R; Kuhn, P;
Indirizzi:
Stanford Univ, Stanford Linear Accelerator Ctr, Stanford, CA 94309 USA Stanford Univ Stanford CA USA 94309 celerator Ctr, Stanford, CA 94309 USA Ohio State Univ, Dept Mol & Cellular Biochem, Columbus, OH 43210 USA Ohio State Univ Columbus OH USA 43210 lar Biochem, Columbus, OH 43210 USA
Titolo Testata:
STRUCTURE
fascicolo: 2, volume: 9, anno: 2001,
pagine: 125 - 132
SICI:
0969-2126(20010207)9:2<125:CSOT1K>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN; REDUCTASE; MOLYBDOPTERIN; RESOLUTION; ENZYMES; PROGRAM; MO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Kuhn, P Stanford Univ, Stanford Linear Accelerator Ctr, Stanford, CA 94309USA Stanford Univ Stanford CA USA 94309 r Ctr, Stanford, CA 94309 USA
Citazione:
P.J. Ellis et al., "Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 angstrom and 2.03 angstrom", STRUCTURE, 9(2), 2001, pp. 125-132

Abstract

Background: Arsenite oxidase from Alcaligenes faecalis NCIB 8687 is a molybdenum/iron protein involved in the detoxification of arsenic. It is induced by the presence of AsO2- (arsenite) and functions to oxidize (AsO2-)-O-III, which binds to essential sulfhydryl groups of proteins and dithiols, to the relatively less toxic (AsO43-)-O-V (arsenate) prior to methylation. Results: Using a combination of multiple isomorphous replacement with anomalous scattering (MIRAS) and multiple-wavelength anomalous dispersion (MAD)methods, the crystal structure of arsenite oxidase was determined to 2.03 Angstrom in a P2(1) crystal form with two molecules in the asymmetric unit and to 1.64 Angstrom in a P1 crystal form with four molecules in the asymmetric unit. Arsenite oxidase consists of a large subunit of 825 residues anda small subunit of approximately 134 residues. The large subunit contains a Mo site, consisting of a Mo atom bound to two pterin cofactors, and a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site. Conclusions: The large subunit of arsenite oxidase is similar to other members of the dimethylsulfoxide (DMSO) reductase family of molybdenum enzymes, particularly the dissimilatory periplasmic nitrate reductase from Desulfovibrio desulfuricans, but is unique in having no covalent bond between the polypeptide and the Mo atom. The small subunit has no counterpart among known Mo protein structures but is homologous to the Rieske [2Fe-2S] protein domain of the cytochrome be, and cytochrome b(6)f complexes and to the Rieske domain of naphthalene 1,2-dioxygenase.

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Documento generato il 29/11/20 alle ore 17:45:08