The three-dimensional structure of the ligand-binding domain of a wild- type bacterial chemotaxis receptor. Structural comparison to the cross- linked mutant forms and conformational changes upon ligand binding

Journal of Biological Chemistry

Volumn 268, Issue 13, 1993, Pages 9787-9792

  Yeh, J I ^a   Biemann, H P ^a   Pandit, J ^a   Koshland, D E ^a   Kim, S H ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RECEPTOR; ASPARTIC ACID; MEMBRANE PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIUM MUTANT; BINDING SITE; CHEMOTAXIS; CRYSTALLOGRAPHY; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN CONFORMATION; RECEPTOR BINDING; SALMONELLA TYPHIMURIUM; SITE DIRECTED MUTAGENESIS; STOICHIOMETRY;

AMINO ACID SEQUENCE; APOPROTEINS; ASPARTIC ACID; BACTERIAL PROTEINS; BINDING SITES; CROSS-LINKING REAGENTS; LIGANDS; MACROMOLECULAR SYSTEMS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, AMINO ACID; SALMONELLA TYPHIMURIUM; SUPPORT, U.S. GOV'T, NON-P.H.S.; SUPPORT, U.S. GOV'T, P.H.S.;

BACTERIA (MICROORGANISMS); SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0027175202     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (0)