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Titolo:
ASSIGNMENTS, SECONDARY STRUCTURE, GLOBAL FOLD, AND DYNAMICS OF CHEMOTAXIS-Y PROTEIN USING 3-DIMENSIONAL AND 4-DIMENSIONAL HETERONUCLEAR (C-13,N-15) NMR-SPECTROSCOPY
Autore:
MOY FJ; LOWRY DF; MATSUMURA P; DAHLQUIST FW; KRYWKO JE; DOMAILLE PJ;
Indirizzi:
AMER CYANAMID CO,LEDERLE LABS,DIV MED RES PEARL RIVER NY 10965 DUPONT MERCK PHARMACEUT CO,CHEM & PHYS SCI WILMINGTON DE 19880 UNIV OREGON,INST MOLEC BIOL EUGENE OR 97403 UNIV OREGON,DEPT CHEM EUGENE OR 97403 UNIV ILLINOIS,DEPT MICROBIOL & IMMUNOL CHICAGO IL 60612
Titolo Testata:
Biochemistry
fascicolo: 35, volume: 33, anno: 1994,
pagine: 10731 - 10742
SICI:
0006-2960(1994)33:35<10731:ASSGFA>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; VICINAL COUPLING-CONSTANTS; ISOTOPICALLY ENRICHED PROTEINS; BACKBONE NUCLEI; BACTERIAL CHEMOTAXIS; 3-DIMENSIONAL STRUCTURE; C-13-ENRICHED PROTEINS; C-13-LABELED PROTEINS; SOLVENT SUPPRESSION; ENERGY MINIMIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
69
Recensione:
Indirizzi per estratti:
Citazione:
F.J. Moy et al., "ASSIGNMENTS, SECONDARY STRUCTURE, GLOBAL FOLD, AND DYNAMICS OF CHEMOTAXIS-Y PROTEIN USING 3-DIMENSIONAL AND 4-DIMENSIONAL HETERONUCLEAR (C-13,N-15) NMR-SPECTROSCOPY", Biochemistry, 33(35), 1994, pp. 10731-10742

Abstract

NMR spectroscopy has been used to study recombinant Escherichia coli CheY, a 128-residue protein involved in regulating bacterial chemotaxis. Heteronuclear three- and four-dimensional (3D and 4D) experiments have provided sequence-specific resonance assignments and quantitation of short-, medium-, and long-range distance restraints from nuclear Overhauser enhancement (NOE) intensities. These distance restraints werefurther supplemented with measurements of three-bond scalar coupling constants to define the local dihedral angles, and with the identification of amide protons undergoing slow solvent exchange from which hydrogen-bonding patterns were identified. The current model structure shows the same global fold of CheY as existing X-ray structures (Volt & Matsumura, 1991; Stock et al. 1993) with a (beta/alpha)(5) motif of five parallel beta-strands at the central core surrounded by three alpha-helices on one face and with two on the opposite side. Heteronuclear N-15-H-1 relaxation experiments are interpreted to show portions of theprotein structure in the Mg2+ binding loop are ill-defined because ofslow motion (chemical exchange) on the NMR time scale. Moreover, the presence of Mg2+ disrupts the salt bridge between the highly conservedLys-109 and Asp-57, the site of phosphorylation.

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Documento generato il 14/07/20 alle ore 10:16:14