Symmetric complexes of GroE chaperonins as part of the functional cycle.
Science
; 265(5172): 656-9, 1994 Jul 29.
Article
en En
| MEDLINE
| ID: mdl-7913554
ABSTRACT
The particular structural arrangement of chaperonins probably contributes to their ability to assist in the folding of proteins. The interaction of the oligomeric bacterial chaperonin GroEL and its cochaperonin, GroES, in the presence of adenosine diphosphate (ADP) forms an asymmetric complex. However, in the presence of adenosine triphosphate (ATP) or its nonhydrolyzable analogs, symmetric complexes were found by electron microscopy and image analysis. The existence of symmetric chaperonin complexes is not predicted by current models of the functional cycle for GroE-mediated protein folding. Because complete folding of a nonnative substrate protein in the presence of GroEL and GroES only occurs in the presence of ATP, but not with ADP, the symmetric chaperonin complexes formed during the GroE cycle are proposed to be functionally significant.
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Banco de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
/
Proteínas de Choque Térmico
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Science
Año:
1994
Tipo del documento:
Article
País de afiliación:
Alemania