A major conformational change in p97 AAA ATPase upon ATP binding.
Mol Cell
; 6(6): 1485-90, 2000 Dec.
Article
em En
| MEDLINE
| ID: mdl-11163220
ABSTRACT
AAA ATPases play central roles in cellular activities. The ATPase p97, a prototype of this superfamily, participates in organelle membrane fusion. Cryoelectron microscopy and single-particle analysis revealed that a major conformational change of p97 during the ATPase cycle occurred upon nucleotide binding and not during hydrolysis as previously hypothesized. Furthermore, our study indicates that six p47 adaptor molecules bind to the periphery of the ring-shaped p97 hexamer. Taken together, these results provide a revised model of how this and possibly other AAA ATPases can translate nucleotide binding into conformational changes of associated binding partners.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Nucleares
/
Trifosfato de Adenosina
/
Adenosina Trifosfatases
/
Proteínas de Transporte Vesicular
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
Mol Cell
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Estados Unidos