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Titolo:
THE CRYSTAL-STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2-ANGSTROMRESOLUTION
Autore:
XUE YF; LIPSCOMB WN; GRAF R; SCHNAPPAUF G; BRAUS G;
Indirizzi:
HARVARD UNIV,GIBBS CHEM LAB,12 OXFORD ST CAMBRIDGE MA 02138 HARVARD UNIV,GIBBS CHEM LAB CAMBRIDGE MA 02138 ETH ZURICH,INST MIKROBIOL CH-8092 ZURICH SWITZERLAND
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 23, volume: 91, anno: 1994,
pagine: 10814 - 10818
SICI:
0027-8424(1994)91:23<10814:TCOACM>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
CLAISEN REARRANGEMENT; TRANSITION-STATE; PREPHENATE;
Keywords:
ALLOSTERIC PROTEIN; EFFECTOR BINDING; GREEK KEY HELIX BUNDLES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
Y.F. Xue et al., "THE CRYSTAL-STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2-ANGSTROMRESOLUTION", Proceedings of the National Academy of Sciences of the United Statesof America, 91(23), 1994, pp. 10814-10818

Abstract

The crystal structure of an allosteric chorismate mutase, the Thr-226--> Re mutant, from yeast Saccharomyces cerevisiae has been determined to 2.2-Angstrom resolution by using the multiple isomorphous replacement method. Solvent-flattening and electron density modification wereapplied for phase improvement, The current crystallographic R factor is 0.196. The final model includes 504 of the 512 residues and 97 water molecules. In addition, two tryptophan molecules were identified in the interface between monomers. The overall structure is completely different from the reported structure of chorismate mutase from Bacillussubtilis. This structure showed 71% helices with essentially no beta-sheet structures.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 07:41:53