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Article

ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release.

Journal of bacteriology - 1 Oct 2001

Barthel T K, Zhang J, Walker G C

Abstract excerpt

We have characterized the effects of the T199S, T199A, and K70A mutations on the biochemical activity and in vivo functioning of Escherichia coli DnaK. Threonine-199 is the site of autophosphorylation of DnaK, and the lysine residue of bovine Hsc70 corresponding to K70 of DnaK has been shown to be essential for the hydrolysis of ATP. The dnaK alleles T199A and K70A are completely unable, and the T199S allele is...

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Identifiers

PMID: 11544208
DOI: 10.1128/JB.183.19.5482-5490.2001
PMCID: PMC95437

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Source receipt: pubmed, retrieved 7 Sept 2026.

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