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Titolo:
The 1.9 angstrom resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY
Autore:
Halkides, CJ; McEvoy, MM; Casper, E; Matsumura, P; Volz, K; Dahlquist, FW;
Indirizzi:
Univ Illinois, Dept Microbiol & Immunol, Chicago, IL 60612 USA Univ Illinois Chicago IL USA 60612 obiol & Immunol, Chicago, IL 60612 USA Univ N Carolina, Dept Chem, Wilmington, NC 28403 USA Univ N Carolina Wilmington NC USA 28403 pt Chem, Wilmington, NC 28403 USA Univ Oregon, Inst Mol Biol, Dept Chem, Eugene, OR 97403 USA Univ Oregon Eugene OR USA 97403 Mol Biol, Dept Chem, Eugene, OR 97403 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 18, volume: 39, anno: 2000,
pagine: 5280 - 5286
SICI:
0006-2960(20000509)39:18<5280:T1ARCS>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
FLAGELLAR SWITCH PROTEIN; PHOSPHORYLATION-DEPENDENT BINDING; BACTERIAL CHEMOTAXIS; SIGNAL-TRANSDUCTION; UNCOUPLED PHOSPHORYLATION; KINASE CHEA; DOMAIN; FLIM; REFINEMENT; ACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Dahlquist, FW Univ Illinois, Dept Microbiol & Immunol, M-C 790,E-704 Med Sci Bldg,835 S Wolcott Ave, Chicago, IL 60612 USA Univ Illinois M-C 790,E-704 Med Sci Bldg,835 S Wolcott Ave Chicago IL USA 60612
Citazione:
C.J. Halkides et al., "The 1.9 angstrom resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY", BIOCHEM, 39(18), 2000, pp. 5280-5286

Abstract

To structurally characterize the activated state of the transiently phosphorylated signal transduction protein CheY, we have constructed an alpha-thiophosphonate derivative of the CheY D57C point mutant and determined its three-dimensional structure at 1.85 A resolution. We have also characterized this analogue with high-resolution NMR and studied its binding to a peptidederived from FliM, CheY's target component of the flagellar motor. The chemically modified derivative, phosphono-CheY, exhibits many of the chemical properties of phosphorylated wild-type CheY, except that it is indefinitelystable. Electron density for the alpha-thiophosphonate substitution is clear and readily interpretable; omit refinement density at the phosphorus atom is greater than 10 sigma. The molecule shows a number of localized conformational changes that are believed to constitute the postphosphorylation activation events. The most obvious of these changes include movement of the side chain of the active site base, Lys 109, and a predominately buried conformation of the side chain of Tyr 106. In addition, there are a number of more subtle changes more distant from the active site involving the alpha 14 and alpha 5 helices. These results are consistent with our previous structural interpretations of other CheY activation mutants, and with our earlier hypotheses concerning CheY activation through propagation of structural changes away from the active site.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 06:37:32