Structural and enzymatic insights into the ATP binding and autophosphorylation mechanism of a sensor histidine kinase

Journal of Biological Chemistry

Volumn 285, Issue 32, 2010, Pages 24892-24903

  Trajtenberg, Felipe ^a   Graña, Martin ^a   Ruétalo, Natalia ^a   Botti, Horacio ^a   Buschiazzo, Alejandro ^a,b  

^a INSTITUT PASTEUR DE MONTEVIDEO   (Uruguay)

^b INSTITUT PASTEUR   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOLOGY; BIOCHEMICAL ENGINEERING; GENETIC ENGINEERING; PHOSPHATASES; PROTEINS; SENSORS;

ATP-BINDING; AUTOPHOSPHORYLATION; BACILLUS SUBTILIS; BIOCHEMICAL STUDIES; COLD SHOCK; COMPACT STRUCTURES; DOMAIN GEOMETRY; DOMAIN-DOMAIN INTERACTIONS; HIGH RESOLUTION; HISTIDINE KINASE; INTERMEDIATE STATE; MOLECULAR FEATURE; MOLECULAR LEVELS; MOLECULAR SURFACES; NITROGEN METABOLISM; PHOSPHO-TRANSFER; POINT MUTAGENESIS; PROTEIN ENGINEERING; PROTEIN-PROTEIN DOCKING; SENSOR KINASE; SEQUENCE CONSERVATION; STRUCTURAL APPROACH; STRUCTURAL INFORMATION; STRUCTURAL ORGANIZATION; STRUCTURE-BASED;

CRYSTAL STRUCTURE;

ADENOSINE TRIPHOSPHATE; DESK PROTEIN; PROTEIN HISTIDINE KINASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; DISULFIDE; PROTEIN BINDING; PROTEIN KINASE; PROTEIN-HISTIDINE KINASE;

ARTICLE; AUTOPHOSPHORYLATION; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; MOLECULAR DOCKING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN ENGINEERING; PROTEIN PROTEIN INTERACTION; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; BACILLUS SUBTILIS; CHEMISTRY; CONFORMATION; ENZYMOLOGY; KINETICS; MUTAGENESIS; PHOSPHORYLATION; PROCEDURES; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SIGNAL TRANSDUCTION;

ADENOSINE TRIPHOSPHATE; BACILLUS SUBTILIS; BACTERIAL PROTEINS; CATALYSIS; DISULFIDES; KINETICS; MOLECULAR CONFORMATION; MUTAGENESIS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN KINASES; PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION;

EID: 77955296275     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.147843     Document Type: Article

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