Structure of the constitutively active double mutant CheY D13K Y106W alone and in complex with a FliM peptide

Journal of Molecular Biology

Volumn 342, Issue 4, 2004, Pages 1325-1335

  Dyer, Collin M ^a   Quillin, Michael L ^a   Campos, Andres ^b   Lu, Justine ^b   McEvoy, Megan M ^a   Hausrath, Andrew C ^a   Westbrook, Edwin M ^c   Matsumura, Philip ^b,c   Matthews, Brian W ^a   Dahlquist, Frederick W ^a  

^a UNIVERSITY OF OREGON   (United States)

^b UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^c Molecular Biology Consortium   (United States)

Author keywords

activating mutation; chemotaxis; CheY; FliM; protein protein interactions

Indexed keywords

AMINO ACID; ASPARTIC ACID; CHEY PROTEIN; FLIM 16 PROTEIN; ISOLEUCINE; LYSINE; MUTANT PROTEIN; PROTEIN; REGULATOR PROTEIN; SELENOMETHIONINE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; DERIVATIZATION; FLAGELLUM; LIGAND BINDING; MOLECULE; PHENOTYPE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; PROTEIN TARGETING; R FACTOR; WILD TYPE;

EID: 4544243344     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.07.084     Document Type: Article

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