Structure of the M. tuberculosis DnaK−GrpE complex reveals how key DnaK roles are controlled
Structure of the M. tuberculosis DnaK−GrpE complex reveals how key DnaK roles are controlled
About this item
Full title
Author / Creator
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
Formats
Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
The molecular chaperone DnaK is essential for viability of
Mycobacterium tuberculosis
(Mtb). DnaK hydrolyzes ATP to fold substrates, and the resulting ADP is exchanged for ATP by the nucleotide exchange factor GrpE. It has been unclear how GrpE couples DnaK’s nucleotide exchange with substrate release. Here we report a cryo-EM analysis of Grp...
Alternative Titles
Full title
Structure of the M. tuberculosis DnaK−GrpE complex reveals how key DnaK roles are controlled
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_e7c37212224c4be3917a29c7faaee85f
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e7c37212224c4be3917a29c7faaee85f
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-024-44933-9
