Ontology highlight
ABSTRACT:
SUBMITTER: Xiao X
PROVIDER: S-EPMC10803776 | biostudies-literature | 2024 Jan
REPOSITORIES: biostudies-literature
Xiao Xiansha X Fay Allison A Molina Pablo Santos PS Kovach Amanda A Glickman Michael S MS Li Huilin H
Nature communications 20240122 1
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 GrpE bound to an intact Mtb DnaK, revealing an asymmetric 1:2 DnaK-GrpE complex. The GrpE dimer ratchets to modulate both DnaK nucleotide-binding domain and th ...[more]