6W6E

The Mycobacterium tuberculosis ClpB disaggregase hexamer structure with a locally refined ClpB middle domain and a DnaK nucleotide binding domain

6W6E の概要

• エントリーDOI: 10.2210/pdb6w6e/pdb
• EMDBエントリー: 21553 21554 21555 21556 21557
• 分子名称: Chaperone protein ClpB, Chaperone protein DnaK, Substrate, ... (5 entities in total)
• 機能のキーワード: clpb-dnak complex, disaggregate, unfold, refold, chaperone
• 由来する生物種: Mycobacterium tuberculosis; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 631953.71

構造登録者

Yin, Y.,Li, H. (登録日: 2020-03-16, 公開日: 2021-05-26, 最終更新日: 2024-05-29)

主引用文献

Yin, Y.,Feng, X.,Yu, H.,Fay, A.,Kovach, A.,Glickman, M.S.,Li, H.
Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.
Cell Rep, 35:109166-109166, 2021

PubMed Abstract: 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, identify a conserved TGIP loop linking the oligonucleotide/oligosaccharide-binding domain and the nucleotide-binding domain that is important for ClpB function, derive the interface between the regulatory middle domain of the ClpB and the DnaK nucleotide-binding domain, and find that DnaK binding stabilizes, but does not bend or tilt, the ClpB middle domain. We propose a model for the synergistic actions of aggregate dissolution and refolding by the Mtb ClpB-DnaK bi-chaperone system.

PubMed: 34038719
DOI: 10.1016/j.celrep.2021.109166

実験手法

ELECTRON MICROSCOPY (3.7 Å)