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Title: Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1

Abstract

Classic Hsp70 chaperones assist in diverse processes of protein folding and translocation, and Hsp110s had seemed by sequence to be distant relatives within an Hsp70 superfamily. The 2.4 Angstroms resolution structure of Sse1 with ATP shows that Hsp110s are indeed Hsp70 relatives, and it provides insight into allosteric coupling between sites for ATP and polypeptide-substrate binding in Hsp70s. Subdomain structures are similar in intact Sse1(ATP) and in the separate Hsp70 domains, but conformational dispositions are radically different. Interfaces between Sse1 domains are extensive, intimate, and conservative in sequence with Hsp70s. We propose that Sse1(ATP) may be an evolutionary vestige of the Hsp70(ATP) state, and an analysis of 64 mutant variants in Sse1 and three Hsp70 homologs supports this hypothesis. An atomic-level understanding of Hsp70 communication between ATP and substrate-binding domains follows. Requirements on Sse1 for yeast viability are in keeping with the distinct function of Hsp110s as nucleotide exchange factors.

Authors:
;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
959566
Report Number(s):
BNL-82552-2009-JA
Journal ID: ISSN 0092-8674; CELLB5; TRN: US201016%%710
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Cell; Journal Volume: 131
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; COMMUNICATIONS; CRYSTAL STRUCTURE; HYPOTHESIS; MUTANTS; NUCLEOTIDES; PROTEINS; RESOLUTION; TRANSLOCATION; VIABILITY; YEASTS; national synchrotron light source

Citation Formats

Liu,Q., and Hendrickson, W. Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1. United States: N. p., 2007. Web. doi:10.1016/j.cell.2007.08.039.
Liu,Q., & Hendrickson, W. Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1. United States. doi:10.1016/j.cell.2007.08.039.
Liu,Q., and Hendrickson, W. Mon . "Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1". United States. doi:10.1016/j.cell.2007.08.039.
@article{osti_959566,
title = {Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1},
author = {Liu,Q. and Hendrickson, W.},
abstractNote = {Classic Hsp70 chaperones assist in diverse processes of protein folding and translocation, and Hsp110s had seemed by sequence to be distant relatives within an Hsp70 superfamily. The 2.4 Angstroms resolution structure of Sse1 with ATP shows that Hsp110s are indeed Hsp70 relatives, and it provides insight into allosteric coupling between sites for ATP and polypeptide-substrate binding in Hsp70s. Subdomain structures are similar in intact Sse1(ATP) and in the separate Hsp70 domains, but conformational dispositions are radically different. Interfaces between Sse1 domains are extensive, intimate, and conservative in sequence with Hsp70s. We propose that Sse1(ATP) may be an evolutionary vestige of the Hsp70(ATP) state, and an analysis of 64 mutant variants in Sse1 and three Hsp70 homologs supports this hypothesis. An atomic-level understanding of Hsp70 communication between ATP and substrate-binding domains follows. Requirements on Sse1 for yeast viability are in keeping with the distinct function of Hsp110s as nucleotide exchange factors.},
doi = {10.1016/j.cell.2007.08.039},
journal = {Cell},
number = ,
volume = 131,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}