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Titolo:
CRYSTAL-STRUCTURE OF THE T-STATE OF ALLOSTERIC YEAST CHORISMATE MUTASE AND COMPARISON WITH THE R-STATE
Autore:
STRATER N; HAKANSSON K; SCHNAPPAUF G; BRAUS G; LIPSCOMB WN;
Indirizzi:
HARVARD UNIV,GIBBS CHEM LAB,12 OXFORD ST CAMBRIDGE MA 02138 HARVARD UNIV,GIBBS CHEM LAB CAMBRIDGE MA 02138 UNIV ERLANGEN NURNBERG,INST MIKROBIOL BIOCHEM & GENET D-91058 ERLANGEN GERMANY
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 8, volume: 93, anno: 1996,
pagine: 3330 - 3334
SICI:
0027-8424(1996)93:8<3330:COTTOA>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
CLAISEN REARRANGEMENT; TRANSITION-STATE; PREPHENATE;
Keywords:
ALLOSTERIC ENZYME; ENZYME REGULATION; X-RAY DIFFRACTION; HETEROTROPIC EFFECTOR; CONFORMATIONAL CHANGE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
22
Recensione:
Indirizzi per estratti:
Citazione:
N. Strater et al., "CRYSTAL-STRUCTURE OF THE T-STATE OF ALLOSTERIC YEAST CHORISMATE MUTASE AND COMPARISON WITH THE R-STATE", Proceedings of the National Academy of Sciences of the United Statesof America, 93(8), 1996, pp. 3330-3334

Abstract

The crystal structure of the tyrosine-bound T state of allosteric yeast Saccharomyces cerevisiae chorismate mutase was solved by molecular replacement at a resolution of 2.8 Angstrom using a monomer of the R-state structure as the search model, The allosteric inhibitor tyrosine was found to bind in the T state at the same binding site as the allosteric activator tryptophan binds in the R state, thus defining one regulatory binding site for each monomer. Activation by tryptophan is caused by the larger steric size of its side chain, thereby pushing apartthe allosteric domain of one monomer and helix H8 of the catalytic domain of the other monomer. Inhibition is caused by polar contacts of tyrosine with Arg-75 and Arg-76 of one monomer and with Gly-141, Ser-142, and Thr-145 of the other monomer, thereby bringing the allosteric and catalytic domains closer together. The allosteric transition includes an 8 degrees rotation of each of the two catalytic domains relativeto the allosteric domains of each monomer (domain closure). Alternatively, this transition ran be described as a 15 degrees rotation of thecatalytic domains of the dimer relative to each other.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/07/20 alle ore 20:56:38