7AZP

Structure of the human mitochondrial HSPD1 single ring

7AZP の概要

• エントリーDOI: 10.2210/pdb7azp/pdb
• EMDBエントリー: 11189 11950
• 分子名称: 60 kDa heat shock protein, mitochondrial (1 entity in total)
• 機能のキーワード: hspd1, hsp60, chaperonin, chaperone
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 408148.84

構造登録者

Klebl, D.P.,Feasey, M.C.,Muench, S.P. (登録日: 2020-11-17, 公開日: 2021-02-10, 最終更新日: 2024-05-01)

主引用文献

Klebl, D.P.,Feasey, M.C.,Hesketh, E.L.,Ranson, N.A.,Wurdak, H.,Sobott, F.,Bon, R.S.,Muench, S.P.
Cryo-EM structure of human mitochondrial HSPD1.
Iscience, 24:102022-102022, 2021

PubMed Abstract: Chaperonins play an important role in folding newly synthesized or translocated proteins in all organisms. The bacterial chaperonin GroEL has served as a model system for the understanding of these proteins. In comparison, its human homolog, known as mitochondrial heat shock protein family member D1 (HSPD1) is poorly understood. Here, we present the structure of HSPD1 in the apo state determined by cryo-electron microscopy (cryo-EM). Unlike GroEL, HSPD1 forms mostly single ring assemblies in the absence of co-chaperonin (HSPE1). Comparison with GroEL shows a rotation and increased flexibility of the apical domain. Together with published structures of the HSPD1/HSPE1 co-chaperonin complex, this work gives insight into the structural changes that occur during the catalytic cycle. This new understanding of HSPD1 structure and its rearrangements upon complex formation may provide new insights for the development of HSPD1-targeting treatments against a diverse range of diseases including glioblastoma.

PubMed: 33506187
DOI: 10.1016/j.isci.2020.102022

実験手法

ELECTRON MICROSCOPY (3.5 Å)