A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation

Nature Structural and Molecular Biology

Volumn 11, Issue 11, 2004, Pages 1128-1133

  Sewell, B Trevor ^a   Best, Robert B ^a,d   Chen, Shaoxia ^b,e   Roseman, Alan M ^b,e   Farr, George W ^c   Horwich, Arthur L ^c   Saibil, Helen R ^b  

^a UNIVERSITY OF CAPE TOWN   (South Africa)

^b UNIVERSITY OF LONDON   (United Kingdom)

^c YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^e MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONIN; ESCHERICHIA COLI PROTEIN; MUTANT PROTEIN; PROTEIN SUBUNIT;

ALLOSTERISM; ARTICLE; CHEMICAL STRUCTURE; CRYOELECTRON MICROSCOPY; DISSOCIATION; ELECTRICITY; ENZYME ACTIVITY; ESCHERICHIA COLI; HIGH TEMPERATURE; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; WILD TYPE;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; CHAPERONINS; CRYOELECTRON MICROSCOPY; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROSTATICS; ESCHERICHIA COLI; GROEL PROTEIN; GROES PROTEIN; HYDROLYSIS; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION; TEMPERATURE;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 7544242667     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb844     Document Type: Article

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