The BioGRID | PUBLICATION VIEW

	Cell Oct (2007); 131(1):106-20
Insights into hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1-
Liu Q, Hendrickson WA
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA-
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 A 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-
[PUBMED: 17923091]