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Titolo:
NUCLEAR-MAGNETIC-RESONANCE ASSIGNMENTS AND GLOBAL FOLD OF A CHEY-BINDING DOMAIN IN CHEA, THE CHEMOTAXIS-SPECIFIC KINASE OF ESCHERICHIA-COLI
Autore:
MCEVOY MM; ZHOU HJ; ROTH AF; LOWRY DF; MORRISON TB; KAY LE; DAHLQUIST FW;
Indirizzi:
UNIV OREGON,INST MOLEC BIOL EUGENE OR 97403 UNIV OREGON,INST MOLEC BIOL EUGENE OR 97403 UNIV UTAH,DEPT BIOL SALT LAKE CITY UT 84112 UNIV TORONTO,PROT ENGN NETWORK CTR EXCELLENCE TORONTO ON M5S 1A8 CANADA UNIV TORONTO,DEPT MED GENET TORONTO ON M5S 1A8 CANADA UNIV TORONTO,DEPT BIOCHEM TORONTO ON M5S 1A8 CANADA UNIV TORONTO,DEPT CHEM TORONTO ON M5S 1A8 CANADA
Titolo Testata:
Biochemistry
fascicolo: 42, volume: 34, anno: 1995,
pagine: 13871 - 13880
SICI:
0006-2960(1995)34:42<13871:NAAGFO>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
MULTIPLE-QUANTUM COHERENCE; SIDE-CHAIN RESONANCES; BACTERIAL CHEMOTAXIS; SIGNAL TRANSDUCTION; CRYSTAL-STRUCTURE; 3-DIMENSIONAL STRUCTURES; C-13 MAGNETIZATION; COUPLING-CONSTANTS; HYDROGEN-EXCHANGE; BACILLUS-SUBTILIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
75
Recensione:
Indirizzi per estratti:
Citazione:
M.M. Mcevoy et al., "NUCLEAR-MAGNETIC-RESONANCE ASSIGNMENTS AND GLOBAL FOLD OF A CHEY-BINDING DOMAIN IN CHEA, THE CHEMOTAXIS-SPECIFIC KINASE OF ESCHERICHIA-COLI", Biochemistry, 34(42), 1995, pp. 13871-13880

Abstract

CheA is the histidine autokinase in the Escherichia coli chemotaxis signal transduction pathway responsible for coupling of signals received by transmembrane receptors to the response regulators CheY and CheB. Here NMR spectroscopy is used to study a 14 kDa fragment of CheA, residues 124-257, that binds the response regulator CheY. Backbone atom resonance assignments were obtained by analysis of 3D HNCACB, 3D CBCA(CO)NH, and HNCO spectra, whereas side-chain assignments were obtained primarily by analysis of 3D H(CCO)NH, 3D C(CO)NH, 3D HCCH-TOCSY, and 3DH-1,N-15 TOCSY-HSMQC spectra. NOE cross peak patterns and intensitiesas well as torsion angle restraints were used to determine the secondary structure, and a low-resolution structure was calculated by hybriddistance-geometry simulated annealing methods. The CheA124-257 fragment consists of four antiparallel beta strands and two helices, arranged in an ''open-faced beta-sandwich'' motif, as well as two unstructured ends that correspond to domain linkers in the full-length protein. The N-15-H-1 correlation spectrum of N-15-labeled CheA124-257 bound to unlabeled CheY shows specific localized changes that may correspond toa CheY-binding face on CheA.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 22:41:56