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

@article{citeulike:2234038, abstract = {Summary 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.}, author = {Liu, Qinglian and Hendrickson, Wayne A. }, citeulike-article-id = {2234038}, comment = {we first report the structure of Sse1 at 2.4 \r{A} resolution as a complex with ATP. Structures within pieces of this holo Hsp110 are highly similar to those in isolated NBD and SBD portions of Hsp70s, but dramatic conformational rearrangements distinguish each half from its Hsp70 counterpart.}, doi = {10.1016/j.cell.2007.08.039}, journal = {Cell}, keywords = {allostery, chaperone, xray-crystal-structure}, month = {October}, number = {1}, pages = {106--120}, posted-at = {2008-01-15 08:04:52}, priority = {2}, title = {Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1}, url = {http://dx.doi.org/10.1016/j.cell.2007.08.039}, volume = {131}, year = {2007} }

TY - JOUR ID - citeulike:2234038 L3 - citeulike-article-id:2234038 TI - Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1 JF - Cell VL - 131 IS - 1 SP - 106 EP - 120 N2 - Summary 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. KW - allostery KW - chaperone KW - xray-crystal-structure N1 - we first report the structure of Sse1 at 2.4 Å resolution as a complex with ATP. Structures within pieces of this holo Hsp110 are highly similar to those in isolated NBD and SBD portions of Hsp70s, but dramatic conformational rearrangements distinguish each half from its Hsp70 counterpart. AU - Liu, Qinglian AU - Hendrickson, Wayne PY - 2007/10/05/ UR - http://dx.doi.org/10.1016/j.cell.2007.08.039 ER -