Keeping signals straight in phosphorelay signal transduction

Journal of Bacteriology

Volumn 183, Issue 17, 2001, Pages 4941-4949

  Hoch, J A ^a   Varughese, K I ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AUTOKINASE; BACTERIAL ENZYME; BACTERIAL PROTEIN; PHOSPHORELAY PROTEIN; PHOSPHOTRANSFERASE; SENSOR KINASE; UNCLASSIFIED DRUG;

BACTERIAL GENETICS; BACTERIAL GROWTH; BACTERIAL METABOLISM; GENE EXPRESSION; MOLECULAR EVOLUTION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SHORT SURVEY; SIGNAL TRANSDUCTION; SPOROGENESIS;

AMINO ACID SEQUENCE; ANIMALS; BACTERIAL PROTEINS; HUMANS; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN CONFORMATION; SIGMA FACTOR; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS;

BACTERIA (MICROORGANISMS);

EID: 0034879819     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.183.17.4941-4949.2001     Document Type: Short Survey

References (18)

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12. Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ
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14. Central role of the BvgS receiver as a phosphorylated intermediate in a complex two-component phosphorelay
15. Integration of multiple domains in a two-component sensor protein: The Bordetella pertussis BvgAS phosphorelay
16. Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase
17. A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction
18. NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: Assignments, secondary structure, general fold, and backbone dynamics