Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.
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ABSTRACT:
SUBMITTER: Yin Y
PROVIDER: S-EPMC8209680 | biostudies-literature | 2021 May
REPOSITORIES: biostudies-literature
Publications
Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.
Yin Yanting Y Feng Xiang X Yu Hongjun H Fay Allison A Kovach Amanda A Glickman Michael S MS Li Huilin H
Cell reports 20210501 8
The M. tuberculosis (Mtb) ClpB is a protein disaggregase that helps to rejuvenate the bacterial cell. DnaK is a protein foldase that can function alone, but it can also bind to the ClpB hexamer to physically couple protein disaggregation with protein refolding, although the molecular mechanism is not well understood. Here, we report the cryo-EM analysis of the Mtb ClpB-DnaK bi-chaperone in the presence of ATPγS and a protein substrate. We observe three ClpB conformations in the presence of DnaK, ...[more]
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