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Article

Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate.

Proceedings of the National Academy of Sciences of the United States of America - 26 May 2009

Bertelsen Eric B, Chang Lyra, Gestwicki Jason E, Zuiderweg Erik R P

Abstract excerpt

DnaK is the canonical Hsp70 molecular chaperone protein from Escherichia coli. Like other Hsp70s, DnaK comprises two main domains: a 44-kDa N-terminal nucleotide-binding domain (NBD) that contains ATPase activity, and a 25-kDa substrate-binding domain (SBD) that harbors the substrate-binding site. Here, we report an experimental structure for wild-type, full-length DnaK, complexed with the peptide NRLLLTG and...

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Identifiers

PMID: 19439666
DOI: 10.1073/pnas.0903503106
PMCID: PMC2689011

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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