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Titolo:
STRUCTURE AND DYNAMICS OF A CHEY-BINDING DOMAIN OF THE CHEMOTAXIS KINASE CHEA DETERMINED BY NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY
Autore:
MCEVOY MM; MUHANDIRAM DR; KAY LE; DAHLQUIST FW;
Indirizzi:
UNIV OREGON,INST MOLEC BIOL EUGENE OR 97403 UNIV OREGON,INST MOLEC BIOL EUGENE OR 97403 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 UNIV TORONTO,PROT ENGN NETWORK CTR EXCELLENCE TORONTO ON M5S 1A8 CANADA
Titolo Testata:
Biochemistry
fascicolo: 18, volume: 35, anno: 1996,
pagine: 5633 - 5640
SICI:
0006-2960(1996)35:18<5633:SADOAC>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
MODEL-FREE APPROACH; SIGNAL-TRANSDUCTION; BACTERIAL CHEMOTAXIS; BACKBONE DYNAMICS; NMR-SPECTROSCOPY; PHOSPHORYLATION; MACROMOLECULES; RELAXATION; PROTEINS; SYSTEM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
M.M. Mcevoy et al., "STRUCTURE AND DYNAMICS OF A CHEY-BINDING DOMAIN OF THE CHEMOTAXIS KINASE CHEA DETERMINED BY NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY", Biochemistry, 35(18), 1996, pp. 5633-5640

Abstract

The Escherichia coli histidine autokinase CheA plays an important role in coupling signals received from membrane-bound receptors to changes in the swimming behavior of the cells in order to respond appropriately to environmental signals. Here we describe the structure of the 14kDa fragment of the chemotaxis kinase CheA, residues 124-257, which binds to the downstream targets of phosphorylation, the response regulators CheY and CheB. This protein fragment contains the CheY-binding domain flanked on each side by regions that correspond to domain linkersin the intact protein, The structure of the domain was determined from 1429 restraints derived from heteronuclear multidimensional NMR experiments. Hybrid distance geometry-dynamical simulated annealing methods were use to calculate a family of structures that satisfy the experimental distance restraints and torsion angle restraints. The root meansquare deviation of the 69 ordered residues in the domain is 0.52 Angstrom for the backbone heavy atoms and 0.99 Angstrom for all heavy atoms. The residues that have been implicated as important for CheY binding form a face consisting of several partially buried hydrophobic residues, framed by charged residues. The dynamic properties of this protein fragment were measured and analyzed using both isotropic and anisotropic models of molecular motion, The linker regions are very flexibleand disordered, as evidenced by the very different dynamics properties as compared to the CheY-binding domain, The CheY-binding domain of CheA is structurally similar to the histidine-containing phosphocarrier, HPr, which is a protein involved in the phosphoenolpyruvate:sugar phosphotransferase (PTS) pathway. This structural similarity suggests a possible evolutionary relationship of the PTS and chemotaxis pathways.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 09:55:59