9IP0

Cryo-EM structure of ClpB1 heptamer from Oryza sativa

9IP0 の概要

• エントリーDOI: 10.2210/pdb9ip0/pdb
• EMDBエントリー: 60751
• 分子名称: Chaperone protein ClpB1, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: osclpb, plant protein
• 由来する生物種: Oryza sativa subsp. japonica (rice)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 713300.13

構造登録者

Jobichen, C.,Saharan, K.,Vasudevan, D.,Sivaraman, J. (登録日: 2024-07-10, 公開日: 2025-05-14, 最終更新日: 2025-06-18)

主引用文献

Jobichen, C.,Saharan, K.,Samal, A.,Choong, Y.K.,Jagdev, M.K.,Mohapatra, C.,Jian, S.,Babbar, R.,Dobson, R.C.J.,Grover, A.,Vasudevan, D.,Sivaraman, J.
Cryo-EM structure provides insights into the unusual heptameric assembly of rice (Oryza sativa L.) ClpB1 AAA+ ATPase.
Int.J.Biol.Macromol., 311:143917-143917, 2025

PubMed Abstract: Heat stress disrupts the protein homeostasis leading to the accumulation of toxic aggregated proteins in the cell. ClpB disaggregase belonging to the AAA+ ATPase superfamily removes the aggregated toxic proteins. ClpB is present ubiquitously in bacteria, yeast, protozoans and plants and plays a role in acquired heat tolerance. This study was focused on cytoplasmic ClpB1 from rice which is the staple food for more than half of world's population. In bacteria and yeast, ClpB forms a hexameric assembly for carrying out the disaggregase function, however, none of the plant ClpB isoforms have been structurally characterized. Here, we report the cryo-EM structure of ClpB1 from rice (Oryza sativa L.; OsClpB1) at 4 Å resolution. The structure reveals that OsClpB1 assembles as an unusual heptameric ring, possibly representing a non-processive open conformation. Our results point to the structural plasticity of OsClpB1 since it exists in different oligomeric forms. Analytical ultracentrifugation studies confirmed OsClpB1 exist as a heptamer in solution as well, suggesting the presence of the heptameric form of OsClpB1 within the cellular milieu of the rice plant.

PubMed: 40324502
DOI: 10.1016/j.ijbiomac.2025.143917

実験手法

ELECTRON MICROSCOPY (4 Å)