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Titolo:
2 BINDING MODES REVEAL FLEXIBILITY IN KINASE RESPONSE REGULATOR INTERACTIONS IN THE BACTERIAL CHEMOTAXIS PATHWAY/
Autore:
MCEVOY MM; HAUSRATH AC; RANDOLPH GB; REMINGTON SJ; DAHLQUIST FW;
Indirizzi:
UNIV OREGON,INST MOL BIOL,DEPT CHEM EUGENE OR 97403 UNIV OREGON,INST MOL BIOL,DEPT CHEM EUGENE OR 97403 UNIV OREGON,DEPT PHYS EUGENE OR 97403
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 13, volume: 95, anno: 1998,
pagine: 7333 - 7338
SICI:
0027-8424(1998)95:13<7333:2BMRFI>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; SIGNAL-TRANSDUCTION; SECONDARY STRUCTURE; PROTEIN CHEY; KINASE CHEA; GLOBAL FOLD; RESONANCE; SURFACE; DOMAIN; NMR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
M.M. Mcevoy et al., "2 BINDING MODES REVEAL FLEXIBILITY IN KINASE RESPONSE REGULATOR INTERACTIONS IN THE BACTERIAL CHEMOTAXIS PATHWAY/", Proceedings of the National Academy of Sciences of the United Statesof America, 95(13), 1998, pp. 7333-7338

Abstract

The crystal structure at 2.0 Angstrom resolution of the complex of the Escherichia coli chemotaxis response regulator CheY and the phosphoacceptor-binding domain (P2) of the kinase CheA is presented. The binding interface involves the fourth and fifth helices and fifth beta-strand of CheY and both helices of P2. Surprisingly, the two heterodimers in the asymmetric unit have two different binding modes involving the same interface, suggesting some flexibility in the binding regions. Significant conformational changes have occurred in CheY compared with previously determined unbound structures, The active site of CheY is exposed by the binding of the kinase domain, possibly to enhance phosphotransfer from CheA to CheY, The conformational changes upon complex formation as well as the observation that there are two different binding modes suggest that the plasticity of CheY is an essential feature ofresponse regulator function.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 19:15:42