Nucleotide binding activity of SecA homodimer is conformationally regulated by temperature and altered by prlD and azi mutations

Journal of Biological Chemistry

Volumn 275, Issue 20, 2000, Pages 15440-15448

  Schmidt, Marcel ^a   Ding, Haiyuan ^a   Ramamurthy, Visvanathan ^a,b   Mukerji, Ishita ^a   Oliver, Donald ^a  

^a WESLEYAN UNIVERSITY   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; NUCLEOTIDE BINDING PROTEIN;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; GENE MUTATION; PRIORITY JOURNAL; PROTEIN TRANSPORT; STRUCTURE ACTIVITY RELATION; TEMPERATURE;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; AZIDES; BACTERIAL PROTEINS; BINDING SITES; CARRIER PROTEINS; DIMERIZATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; MEMBRANE TRANSPORT PROTEINS; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN SORTING SIGNALS; RECOMBINANT PROTEINS; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 0034686046     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M000605200     Document Type: Article

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