An interaction between the walker A and D-loop motifs is critical to ATP hydrolysis and cooperativity in bacteriophage T4 Rad50

Journal of Biological Chemistry

Volumn 286, Issue 29, 2011, Pages 26258-26266

  De La Rosa, Metzere Bierlein ^a,b   Nelson, Scott W ^a  

^a IOWA STATE UNIVERSITY   (United States)

^b GRINNELL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE RESIDUE; ASPARTATES; ATP HYDROLYSIS; ATP-BINDING CASSETTE; ATP-BINDING SITE; BACTERIOPHAGE T4; CONFORMATIONAL CHANGE; COOPERATIVITY; DIMER INTERFACE; FUNCTIONAL FORMS; HYDROLYSIS RATE; MUTANT PROTEINS; NUCLEASE ACTIVITY; NUCLEOTIDE-BINDING DOMAIN; PHOSPHATE SENSORS;

AMINO ACIDS; BACTERIOPHAGES; CATALYSIS; HYDROLYSIS; PROTEINS;

BINDING SITES;

ADENOSINE TRIPHOSPHATE; ASPARAGINE; ASPARTIC ACID; DNA; MRE11 PROTEIN; MUTANT PROTEIN; NUCLEASE; RAD50 PROTEIN;

ARTICLE; BACTERIOPHAGE T4; BINDING AFFINITY; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; GENE MUTATION; HYDROLYSIS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DNA BINDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; STEADY STATE; WALKER A LOOP MOTIF; WALKER D LOOP MOTIF;

ADENOSINE TRIPHOSPHATE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ASPARTIC ACID; ATP-BINDING CASSETTE TRANSPORTERS; BACTERIOPHAGE T4; BASE SEQUENCE; DNA; DNA-BINDING PROTEINS; EXODEOXYRIBONUCLEASES; HYDROLYSIS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN BINDING; VIRAL PROTEINS;

EID: 79960432641     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.256305     Document Type: Article

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