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Science 23 February 2001:
Vol. 291. no. 5508, p. 1443
DOI: 10.1126/science.291.5508.1443n
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Members of the molecular chaperone 70-kilodalton heat shock protein (Hsp70) family bind and release substrate in a manner dependent on their adenosine triphosphate (ATP) activity. In the bacterial Hsp70 homolog, DnaK, the protein GrpE promotes substrate release by enhancing nucleotide exchange. Sondermann et al. (p. 1563) have now solved the structure at 1.9 angstroms of the Hsp70 ATPase domain bound to a Bag domain that promotes ATP-dependent release of substrate in vitro. Although the Bag domain is structurally unrelated to GrpE, the conformations of the bound ATPase domains of Hsp70 and DnaK are similar. It appears that the nucleotide-release mechanism has been conserved through convergent evolution of the eukaryotic Bag domain.




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Science. ISSN 0036-8075 (print), 1095-9203 (online)