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Titolo:
A structural variation for MurB: X-ray crystal structure of Staphylococcusaureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB)
Autore:
Benson, TE; Harris, MS; Choi, GH; Cialdella, JI; Herberg, JT; Martin, JP; Baldwin, ET;
Indirizzi:
Pharmacia Corp, Struct Analyt & Med Chem Biol & Prot Sci, Kalamazoo, MI 49007 USA Pharmacia Corp Kalamazoo MI USA 49007 & Prot Sci, Kalamazoo, MI 49007 USA Human Genome Sci Inc, Mol Biol, Rockville, MD 20850 USA Human Genome Sci Inc Rockville MD USA 20850 Biol, Rockville, MD 20850 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 8, volume: 40, anno: 2001,
pagine: 2340 - 2350
SICI:
0006-2960(20010227)40:8<2340:ASVFMX>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE; ALANINE-ADDING ENZYME; ESCHERICHIA-COLI; CRYSTALLOGRAPHIC REFINEMENT; PEPTIDOGLYCAN BIOSYNTHESIS; METHICILLIN-RESISTANT; NADP(+) BINDING; OVER-PRODUCTION; S229A MUTANT; D-GLUTAMATE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Benson, TE Pharmacia Corp, Struct Analyt & Med Chem Biol & Prot Sci, 301 Henrietta St, Kalamazoo, MI 49007 USA Pharmacia Corp 301 Henrietta St Kalamazoo MI USA 49007 9007 USA
Citazione:
T.E. Benson et al., "A structural variation for MurB: X-ray crystal structure of Staphylococcusaureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB)", BIOCHEM, 40(8), 2001, pp. 2340-2350

Abstract

The X-ray crystal structure of the substrate free form of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB) has been solved to 2.3 Angstrom resolution with an R-factor of 20.3% and a free R-factor of 22.3%. While the overall fold of the S. aureus enzyme is similar to that ofthe homologous Escherichia coli MurB X-ray crystal structure, notable distinctions between the S. aureus and E. coli MurB protein structures occur inresidues involved in substrate binding. Analysis of available MurB sequences from other bacteria suggest that the S. aureus MurB structure is representative of a distinct structural class of UDP-N-acetylenolpyruvylglucosamine reductases including Bacillus subtilis and Helicobacter pylori that are characterized by a modified mechanism for substrate binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 19:19:09