Cryo-EM 3D map of the Mycobacterium tuberculosis Hsp70 protein DnaK bound to the nucleotide exchange factor GrpE: EMD-29913
UID: 11491
- Description
- Description from EMDB:
"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."
Sample Organism: Mycobacterium tuberculosis
Sample: Binary complex of DnaK with nucleotide exchange factor GrpE
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Access via EMDB
Accession #: EMD-29913 - Access Restrictions
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Free to All
- Access Instructions
- Free to download from EMDB
- DOI
- doi:10.1038/s41467-024-44933-9
- Associated Publications
- Equipment Used
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FEI VITROBOT MARK II
- Dataset Format(s)
- PDF, XML, gzip, CIF, MAP
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