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Titolo:
Structure-based identification of a novel NTPase from Methanococcus jannaschii
Autore:
Hwang, KY; Chung, JH; Kim, SH; Han, YS; Cho, YJ;
Indirizzi:
Korea Inst Sci & Technol, Struct Biol Ctr, Seoul 130650, South Korea KoreaInst Sci & Technol Seoul South Korea 130650 ul 130650, South Korea Korea Univ, Grad Sch Biotechnol, Seoul 136701, South Korea Korea Univ Seoul South Korea 136701 iotechnol, Seoul 136701, South Korea Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA Univ Calif Berkeley Berkeley CA USA 94720 pt Chem, Berkeley, CA 94720 USA Univ Calif Berkeley, EO Lawrence Berkeley Natl Lab, Berkeley, CA 94720 USAUniv Calif Berkeley Berkeley CA USA 94720 atl Lab, Berkeley, CA 94720 USA
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 7, volume: 6, anno: 1999,
pagine: 691 - 696
SICI:
1072-8368(199907)6:7<691:SIOANN>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
COMPLETE GENOME SEQUENCE; TRANSFER-RNA SYNTHETASE; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; SACCHAROMYCES-CEREVISIAE; THERMUS-THERMOPHILUS; PROTEIN; DATABASE; 6-N-HYDROXYLAMINOPURINE; RESOLUTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Cho, YJ Korea Inst Sci & Technol, Struct Biol Ctr, POB 131, Seoul 130650, South Korea Korea Inst Sci & Technol POB 131 Seoul South Korea 130650 h Korea
Citazione:
K.Y. Hwang et al., "Structure-based identification of a novel NTPase from Methanococcus jannaschii", NAT ST BIOL, 6(7), 1999, pp. 691-696

Abstract

Almost half of the entire set of predicted genomic products from Methanococcus jannaschii are classified as functionally unknown hypothetical proteins. We present a structure-based identification of the biochemical function of a protein with an as yet unknown function from a M. jannaschii gene, Mj0226. The crystal structure of Mj0226 protein determined at 2.2 Angstrom, resolution reveals that the protein is a homodimer and each monomer folds into an elongated alpha/beta structure of a new ford family. Comparisons of Mj0226 protein with protein structures in the database, however, indicate that one part of the protein is homologous to some of the nucleotide-binding proteins. Biochemical analysis shows that Mj0226 protein is a novel nucleotide triphosphatase that can efficiently hydrolyze nonstandard nucleotides such as XTP to XMP or ITP to IMP, but not the standard nucleotides, in the presence of Mg2+ or Mn2+ ions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 18:07:47