Functional and structural characterization of RsbU, a stress signaling protein phosphatase 2C

Journal of Biological Chemistry

Volumn 279, Issue 39, 2004, Pages 40927-40937

  Delumeau, Olivier ^a,d   Dutta, Sujit ^a,e   Brigulla, Matthias ^b,c   Kuhnke, Grit ^b,c,f   Hardwick, Steven W ^d   Völker, Uwe ^b,c   Yudkin, Michael D ^a   Lewis, Richard J ^a,d  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b MAX PLANCK INSTITUTE FOR TERRESTRIAL MICROBIOLOGY   (Germany)

^c UNIVERSITY OF GREIFSWALD   (Germany)

^d NEWCASTLE UNIVERSITY   (United Kingdom)

^e NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^f PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BACTERIA; BIOCHEMISTRY; PHOSPHATES; STRESS ANALYSIS;

C-TERMINAL DOMAINS; POSITIVE REGULATORS; SEQUENCE HOMOLOGY; STRESS SIGNALING RECEPTORS;

ENZYMES;

PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2C; PROTEIN; RSBT PROTEIN; RSBU PROTEIN; SIGMA FACTOR; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; BACTERIAL GENE; C TERMINAL DOMAIN; CONSERVED DOMAIN; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVITY; GRAM POSITIVE BACTERIUM; IN VITRO STUDY; IN VIVO STUDY; N TERMINAL DOMAIN; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN STRUCTURE; RSBT GENE; RSBU GENE; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STOICHIOMETRY; STRESS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HYDROGEN BONDING; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHENOTYPE; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORIC MONOESTER HYDROLASES; PLASMIDS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL TRANSDUCTION; TIME FACTORS;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); POSIBACTERIA;

EID: 4644273104     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M405464200     Document Type: Article

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