Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
CRYSTAL-STRUCTURE OF GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE AMIDOTRANSFERASE FROM ESCHERICHIA-COLI
Autore:
MUCHMORE CRA; KRAHN JM; KIM JH; ZALKIN H; SMITH JL;
Indirizzi:
PURDUE UNIV,DEPT BIOL SCI W LAFAYETTE IN 47907 PURDUE UNIV,DEPT BIOL SCI W LAFAYETTE IN 47907 PURDUE UNIV,DEPT BIOCHEM W LAFAYETTE IN 47907
Titolo Testata:
Protein science
fascicolo: 1, volume: 7, anno: 1998,
pagine: 39 - 51
SICI:
0961-8368(1998)7:1<39:COGPA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAY-DIFFRACTION DATA; OROTATE PHOSPHORIBOSYLTRANSFERASE; 5-PHOSPHORIBOSYLPYROPHOSPHATE AMIDOTRANSFERASE; MOLECULAR REPLACEMENT; WEISSENBERG CAMERA; FLEXIBLE LOOP; PURINE; REFINEMENT; SITE; CRYSTALLOGRAPHY;
Keywords:
ALLOSTERIC ENZYME; COMPLEX ENZYME; FEEDBACK INHIBITION; FE-S PROTEIN; GLUTAMINE AMIDOTRANSFERASE; PHOSPHORIBOSYLTRANSFERASE; PROTEIN CRYSTALLOGRAPHY; PURINE BIOSYNTHESIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
C.R.A. Muchmore et al., "CRYSTAL-STRUCTURE OF GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE AMIDOTRANSFERASE FROM ESCHERICHIA-COLI", Protein science, 7(1), 1998, pp. 39-51

Abstract

Crystal structures of glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase from Escherichia coli have been determined to 2.0-Angstrom resolution in the absence of ligands, and to 2.5-Angstrom resolution with the feedback inhibitor AMP bound to the PRPP catalytic site. Glutamine PRPP amidotransferase (GPATase) employs separate catalytic domains to abstract nitrogen from the amide of glutamine and to transfernitrogen to the acceptor substrate PRPP. The unliganded and AMP-boundstructures, which are essentially identical, are interpreted as the inhibited form of the enzyme because the two active sites are disconnected and the PRPP active site is solvent exposed. The structures were compared with a previously reported 3.0-Angstrom structure of the homologous Bacillus subtilis enzyme (Smith JL et al., 1994, Science 264:1427-1433). The comparison indicates a pattern of conservation of peptidestructures involved with catalysis and variability in enzyme regulatory functions. Control of glutaminase activity, communication between the active sites, and regulation by feedback inhibitors are addressed differently by E. coli and B. subtilis GPATases. The E. coli enzyme is a prototype for the metal-free GPATases, whereas the B. subtilis enzyme represents the metal-containing enzymes. The structure of the E. coli enzyme suggests that a common ancestor of the two enzyme subfamiliesmay have included an Fe-S cluster.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 12:28:11