Structure of the Hsp110:Hsc70 nucleotide exchange machine.
Mol Cell
; 31(2): 232-43, 2008 Jul 25.
Article
en En
| MEDLINE
| ID: mdl-18550409
ABSTRACT
Hsp70s mediate protein folding, translocation, and macromolecular complex remodeling reactions. Their activities are regulated by proteins that exchange ADP for ATP from the nucleotide-binding domain (NBD) of the Hsp70. These nucleotide exchange factors (NEFs) include the Hsp110s, which are themselves members of the Hsp70 family. We report the structure of an Hsp110Hsc70 nucleotide exchange complex. The complex is characterized by extensive proteinprotein interactions and symmetric bridging interactions between the nucleotides bound in each partner protein's NBD. An electropositive pore allows nucleotides to enter and exit the complex. The role of nucleotides in complex formation and dissociation, and the effects of the proteinprotein interactions on nucleotide exchange, can be understood in terms of the coupled effects of the nucleotides and proteinprotein interactions on the open-closed isomerization of the NBDs. The symmetrical interactions in the complex may model other Hsp70 family heterodimers in which two Hsp70s reciprocally act as NEFs.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Proteínas del Choque Térmico HSC70
/
Proteínas del Choque Térmico HSP110
/
Nucleótidos
Tipo de estudio:
Prognostic_studies
Límite:
Animals
/
Humans
Idioma:
En
Año:
2008
Tipo del documento:
Article