The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface

Journal of Bacteriology

Volumn 185, Issue 1, 2003, Pages 254-261

  Birck, Catherine ^a,c   Chen, Yinghua ^b   Hulett, F Marion ^b   Samama, Jean Pierre ^a,c  

^a INSTITUT DE PHARMACOLOGIE ET DE BIOLOGIE STRUCTURALE   (France)

^b UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^c INSTITUT DE GÉNÉTIQUE ET DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

OUTER MEMBRANE PROTEIN REGULATOR; PHOP PROTEIN; PROTEIN; PROTEIN DRRD; PROTEIN PHOB; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS SUBTILIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; GENE EXPRESSION; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; POSIBACTERIA; THERMOTOGA; THERMOTOGA MARITIMA;

EID: 0037215598     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.1.254-261.2003     Document Type: Article

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