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TitleStructure of the M. tuberculosis DnaK-GrpE complex reveals how key DnaK roles are controlled.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 660, Year 2024
Publish dateJan 22, 2024
AuthorsXiansha Xiao / Allison Fay / Pablo Santos Molina / Amanda Kovach / Michael S Glickman / Huilin Li /
PubMed AbstractThe 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 ...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 the substrate-binding domain. We further show that the disordered GrpE N-terminus is critical for substrate release, and that the DnaK-GrpE interface is essential for protein folding activity both in vitro and in vivo. Therefore, the Mtb GrpE dimer allosterically regulates DnaK to concomitantly release ADP in the nucleotide-binding domain and substrate peptide in the substrate-binding domain.
External linksNat Commun / PubMed:38253530 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 5.8 Å
Structure data

29912

8gb3

EMDB-29912: Cryo-EM 3D map of the Mycobacterium tuberculosis Hsp70 protein DnaK bound to the nucleotide exchange factor GrpE
PDB-8gb3: Structure of the Mycobacterium tuberculosis Hsp70 protein DnaK bound to the nucleotide exchange factor GrpE
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-29913: Cryo-EM 3D map of the Mycobacterium tuberculosis Hsp70 protein DnaK bound to the nucleotide exchange factor GrpE
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-29914: Cryo-EM 3D focused map of the Mycobacterium tuberculosis Hsp70 protein DnaK SBD domain
Method: EM (single particle) / Resolution: 5.8 Å

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsCHAPERONE / heat shock protein 70 / nucleotide exchange factor / protein folding and refolding

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