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Article

Monitoring conformational heterogeneity of the lid of DnaK substrate-binding domain during its chaperone cycle.

The FEBS journal - 1 Aug 2016

Banerjee Rupa, Jayaraj Gopal Gunanathan, Peter Joshua Jebakumar, Kumar Vignesh, Mapa Koyeli

Abstract excerpt

DnaK or Hsp70 of Escherichia coli is a master regulator of the bacterial proteostasis network. Allosteric communication between the two functional domains of DnaK, the N-terminal nucleotide-binding domain (NBD) and the C-terminal substrate- or peptide-binding domain (SBD) regulate its activity. X-ray crystallography and NMR studies have provided snapshots of distinct conformations of Hsp70 proteins in various...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 27248857
DOI: 10.1111/febs.13769

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PNP

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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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