The structure of the Escherichia coli nucleoside diphosphate kinase reveals a new quaternary architecture for this enzyme family

Proteins: Structure, Function and Genetics

Volumn 67, Issue 3, 2007, Pages 755-765

  Moynié, Lucile ^a   Giraud, Marie France ^a   Georgescauld, Florian ^a   Lascu, Ioan ^a   Dautant, Alain ^a  

^a Institut de Biochimie et Genetique Cellulaires   (France)

Author keywords

Crystal structure; Dimer; Hexamer; Quaternary structure; Tetramer

Indexed keywords

DIMER; ESCHERICHIA COLI PROTEIN; NUCLEOSIDE DIPHOSPHATE KINASE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBUNIT; ESCHERICHIA COLI; GENETIC CONSERVATION; HUMAN; MYXOCOCCUS XANTHUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEOSIDE-DIPHOSPHATE KINASE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MYXOCOCCUS XANTHUS;

EID: 34247248191     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21316     Document Type: Article

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