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Titolo:
CRYSTAL-STRUCTURE OF A BACTERIAL LIPASE FROM CHROMOBACTERIUM-VISCOSUMATCC-6918 REFINED AT 1.6 ANGSTROM RESOLUTION
Autore:
LANG D; HOFMANN B; HAALCK L; HECHT HJ; SPENER F; SCHMID RD; SCHOMBURG D;
Indirizzi:
GESELL BIOTECHNOL FORSCH MBH,DEPT MOL STRUCT RES,MASCHERODER WEG 1 D-38124 BRAUNSCHWEIG GERMANY GESELL BIOTECHNOL FORSCH MBH,DEPT MOL STRUCT RES D-38124 BRAUNSCHWEIGGERMANY UNIV STUTTGART,INST TECH BIOCHEM D-70569 STUTTGART GERMANY INST CHEMO & BIOSENSOR D-48149 MUNSTER GERMANY
Titolo Testata:
Journal of Molecular Biology
fascicolo: 4, volume: 259, anno: 1996,
pagine: 704 - 717
SICI:
0022-2836(1996)259:4<704:COABLF>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTRON-DENSITY MAPS; INTERFACIAL ACTIVATION; PSEUDOMONAS-GLUMAE; X-RAY; TRIACYLGLYCEROL LIPASE; PATTERN-RECOGNITION; PROTEIN STRUCTURES; TRIAD FORMS; CRYSTALLOGRAPHY; CATALYSIS;
Keywords:
CHROMOBACTERIUM VISCOSUM; TRIACYLGLYCEROL-HYDROLASE (LIPASE); X-RAY CRYSTALLOGRAPHY; PSEUDOMONADACEAE; OXYANION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
66
Recensione:
Indirizzi per estratti:
Citazione:
D. Lang et al., "CRYSTAL-STRUCTURE OF A BACTERIAL LIPASE FROM CHROMOBACTERIUM-VISCOSUMATCC-6918 REFINED AT 1.6 ANGSTROM RESOLUTION", Journal of Molecular Biology, 259(4), 1996, pp. 704-717

Abstract

The crystal structure of a lipase from the bacterium Chromobacterium viscosum ATCC 6918 (CVL) has been determined by isomorphous replacement and refined at 1.6 Angstrom resolution to an X-factor of 17.8%. The lipase has the overall topology of an alpha/beta type protein, which was also found for previously determined lipase structures. The catalytic triad of the active center consists of the residues Ser87, Ap263 and His285. These residues are not exposed to the solvent, but a narrow channel connects them with the molecular surface. This conformation isvery similar to the previously reported closed conformation of Pseudomonas glumae lipase (PGL), but superposition of the two lipase structures reveals several conformational differences. r.m.s. deviations greater than 2 Angstrom are found for the C-proportional to-atoms of the polypeptide chains from His15 to Asp28, from Leu49 to Ser54 and from Lys128 to Gln158. Compared to the PGL structure in the CVL structure, three alpha-helical fragments are shorter, one beta-strand is longer andan additional antiparallel beta-sheet is found. In contrast to PGL, CVL displays an oxyanion hole, which is stabilized by the amide nitrogen atoms of Leu17 and Gln88, and a cis-peptide bond between Gln291 and Leu292. CVL contains a Ca2+, like the PGL, which is coordinated by four oxygen atoms from the protein and two water molecules. (C) 1996 Academic Press Limited

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 19:47:10