pH-Dependent Conformational Changes in Bacterial Hsp90 Reveal a Grp94-Like Conformation at pH 6 That Is Highly Active in Suppression of Citrate Synthase Aggregation

Journal of Molecular Biology

Volumn 390, Issue 2, 2009, Pages 278-291

  Krukenberg, Kristin A ^a   Southworth, Daniel R ^a,b   Street, Timothy O ^a,b   Agard, David A ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

conformational dynamics; Hsp90; molecular chaperone; pH dependence; SAXS

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENYLYLIMIDODIPHOSPHATE; CITRATE SYNTHASE; GLUCOSE REGULATED PROTEIN 94; HEAT SHOCK PROTEIN 90; HISTIDINE;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; ENZYME ACTIVITY; HYDROLYSIS; INHIBITION KINETICS; MUTAGENESIS; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS);

EID: 67349184994     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.04.080     Document Type: Article

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