PMID:8855230

Citation	Burkholder, WF, Zhao, X, Zhu, X, Hendrickson, WA, Gragerov, A and Gottesman, ME (1996) Mutations in the C-terminal fragment of DnaK affecting peptide binding. Proc. Natl. Acad. Sci. U.S.A. 93:10632-7
Abstract	Escherichia coli DnaK acts as a molecular chaperone through its ATP-regulated binding and release of polypeptide substrates. Overexpressing a C-terminal fragment (CTF) of DnaK (Gly-384 to Lys-638) containing the polypeptide substrate binding domain is lethal in wild-type E. coli. This dominant-negative phenotype may result from the nonproductive binding of CTF to cellular polypeptide targets of DnaK. Mutations affecting DnaK substrate binding were identified by selecting noncytotoxic CTF mutants followed by in vitro screening. The clustering of such mutations in the three-dimensional structure of CTF suggests the model that loops L1,2 and L4,5 form a rigid core structure critical for interactions with substrate.
Links	PubMed PMC38205
Keywords	Bacterial Proteins/chemistry; Escherichia coli Proteins; Genes, Dominant; Genetic Complementation Test; HSP70 Heat-Shock Proteins/chemistry; HSP70 Heat-Shock Proteins/genetics; Models, Molecular; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Peptide Fragments/chemistry; Point Mutation; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Structure-Activity Relationship
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