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Titolo:
NMR-STUDIES OF THE PHOSPHOTRANSFER DOMAIN OF THE HISTIDINE KINASE CHEA FROM ESCHERICHIA-COLI - ASSIGNMENTS, SECONDARY STRUCTURE, GENERAL FOLD, AND BACKBONE DYNAMICS
Autore:
ZHOU HJ; LOWRY DF; SWANSON RV; SIMON MI; DAHLQUIST FW;
Indirizzi:
UNIV OREGON,INST MOLEC BIOL EUGENE OR 97403 UNIV OREGON,INST MOLEC BIOL EUGENE OR 97403 CALTECH,DEPT BIOL PASADENA CA 91125
Titolo Testata:
Biochemistry
fascicolo: 42, volume: 34, anno: 1995,
pagine: 13858 - 13870
SICI:
0006-2960(1995)34:42<13858:NOTPDO>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
MULTIPLE-QUANTUM COHERENCE; BACTERIAL CHEMOTAXIS; SIGNAL TRANSDUCTION; COUPLING-CONSTANTS; 3-DIMENSIONAL STRUCTURES; PROTEIN-PHOSPHORYLATION; HETERONUCLEAR NMR; CROSS-RELAXATION; H-1-NMR SPECTRA; ALPHA-HELIX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
H.J. Zhou et al., "NMR-STUDIES OF THE PHOSPHOTRANSFER DOMAIN OF THE HISTIDINE KINASE CHEA FROM ESCHERICHIA-COLI - ASSIGNMENTS, SECONDARY STRUCTURE, GENERAL FOLD, AND BACKBONE DYNAMICS", Biochemistry, 34(42), 1995, pp. 13858-13870

Abstract

Multidimensional heteronuclear NMR techniques were applied to study the phosphotransfer domain, residues 1-134, of the histidine kinase CheA, from Escherichia coli, which contains the site of autophosphorylation, His48, Assignments of the backbone amide groups and side chain protons are nearly complete. Our studies show that this protein fragment consists of five alpha-helices (A-E) connected by turns. Analysis of NOE distance restraints provided by two-dimensional (2D) H-1-H-1 and three-dimensional (3D) N-15-edited NOESY spectra using model building and structure calculations indicates that the five helices form an antiparallel helix bundle with near-neighbor connectivity. The amino-terminal four helices are proposed to be arranged in a right-handed manner with helix E packing against helices C and D. From ideal hydrophobic helical packing and structure calculations, the site of autophosphorylation, His48, is nearly fully exposed to the solvent. We measured the NMR relaxation properties of the backbone N-15 nuclei using inverse detected two-dimensional NMR spectroscopy. The protein backbone dynamics studies show that CheA(1-131) is formed into a tight and compact structure with very limited flexibilities both in helices and turns. Structural implications of titration and phosphorylation experiments are briefly discussed.

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Documento generato il 11/07/20 alle ore 04:39:29