Helical shifts generate two distinct conformers in the atomic resolution structure of the CheA phosphotransferase domain from Thermotoga maritima

Journal of Molecular Biology

Volumn 341, Issue 5, 2004, Pages 1283-1294

  Quezada, Cindy M ^a   Grǎdinaru, Cristian ^b   Simon, Melvin I ^a   Bilwes, Alexandrine M ^b   Crane, Brian R ^b  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^b Department of Obstetrics Gynecology   (United States)

Author keywords

chemotaxis; coiled coil; crystallography; histidine kinase; protein dynamics

Indexed keywords

BACTERIAL ENZYME; GLUTAMIC ACID; HISTIDINE; PHOSPHOTRANSFERASE;

AMINO TERMINAL SEQUENCE; ANISOTROPY; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DIFFRACTION; ENERGY; ENZYME STRUCTURE; HYDROGEN BOND; LOW TEMPERATURE; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; THERMOSTABILITY; THERMOTOGA MARITIMA;

BACTERIA (MICROORGANISMS); THERMOTOGA; THERMOTOGA MARITIMA;

EID: 4143077357     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.06.061     Document Type: Article

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