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Título

Structure of the Hsp110:Hsc70 Nucleotide Exchange Machine

Autor Schuermann, Jonathan P.; Jiang, Jianwen; Cuéllar, Jorge; Llorca, Óscar ; Wang, Liping; Giménez, Luis E.; Jin, Suping; Taylor, Alexander B.; Demeler, Borries; Morano, Kevin A.; Hart, P. John; Valpuesta, José M.; Lafer, Eileen M.; Sousa, Rui
Palabras clave Proteins
Nucleotides
Hsp70s
Nucleotide exchange factors (NEFs)
Nucleotide exchange complex
Chaperones
Fecha de publicación 12-jun-2008
EditorElsevier
Citación Molecular Cell 31(2): 232-243 (2008)
ResumenHsp70s 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 Hsp110:Hsc70 nucleotide exchange complex. The complex is characterized by extensive protein:protein 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 protein:protein interactions on nucleotide exchange, can be understood in terms of the coupled effects of the nucleotides and protein:protein 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.
Descripción 12 pages, 6 figures.-- PMID: 18550409 [PubMed].-- Supplementary information (Suppl. figures S1-S4, 5 pages, and suppl. movie S1, Conformational Changes Induced by Complex Formation) available at the online paper site.
Printed version published on Jul 25, 2008.-- Coordinates and structure factors have been deposited in the RCSB Protein Data Bank with accession code 3C7N.
Versión del editorhttp://dx.doi.org/10.1016/j.molcel.2008.05.006
URI http://hdl.handle.net/10261/9527
DOI10.1016/j.molcel.2008.05.006
ISSN1097-2765
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