An Interdomain Energetic Tug-of-War Creates the Allosterically Active State in Hsp70 Molecular Chaperones
Author:
Publisher
Elsevier BV
Subject
General Biochemistry, Genetics and Molecular Biology
Reference78 articles.
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2. Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate;Bertelsen;Proc. Natl. Acad. Sci. USA,2009
3. Allostery in Hsp70 chaperones is transduced by subdomain rotations;Bhattacharya;J. Mol. Biol.,2009
4. Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication;Buchberger;J. Biol. Chem.,1995
5. Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone;Bukau;EMBO J.,1990
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