7L7S

Human mitochondrial chaperonin mHsp60

7L7S の概要

• エントリーDOI: 10.2210/pdb7l7s/pdb
• EMDBエントリー: 23217
• 分子名称: 60 kDa heat shock protein, mitochondrial (1 entity in total)
• 機能のキーワード: mhsp60, groel, chaperonin, chaperone, isomerase
• 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: 391027.96

構造登録者

Chen, L.,Wang, J.C.Y. (登録日: 2020-12-30, 公開日: 2021-08-25, 最終更新日: 2024-05-29)

主引用文献

Wang, J.C.,Chen, L.
Structural basis for the structural dynamics of human mitochondrial chaperonin mHsp60.
Sci Rep, 11:14809-14809, 2021

PubMed Abstract: Human mitochondrial chaperonin mHsp60 is essential for mitochondrial function by assisting folding of mitochondrial proteins. Unlike the double-ring bacterial GroEL, mHsp60 exists as a heptameric ring that is unstable and dissociates to subunits. The structural dynamics has been implicated for a unique mechanism of mHsp60. We purified active heptameric mHsp60, and determined a cryo-EM structure of mHsp60 heptamer at 3.4 Å. Of the three domains, the equatorial domains contribute most to the inter-subunit interactions, which include a four-stranded β sheet. Our structural comparison with GroEL shows that mHsp60 contains several unique sequences that directly decrease the sidechain interactions around the β sheet and indirectly shorten β strands by disengaging the backbones of the flanking residues from hydrogen bonding in the β strand conformation. The decreased inter-subunit interactions result in a small inter-subunit interface in mHsp60 compared to GroEL, providing a structural basis for the dynamics of mHsp60 subunit association. Importantly, the unique sequences are conserved among higher eukaryotic mitochondrial chaperonins, suggesting the importance of structural dynamics for eukaryotic chaperonins. Our structural comparison with the single-ring mHsp60-mHsp10 shows that upon mHsp10 binding the shortened inter-subunit β sheet is restored and the overall inter-subunit interface of mHsp60 increases drastically. Our structural basis for the mHsp10 induced stabilization of mHsp60 subunit interaction is consistent with the literature that mHsp10 stabilizes mHsp60 quaternary structure. Together, our studies provide structural bases for structural dynamics of the mHsp60 heptamer and for the stabilizing effect of mHsp10 on mHsp60 subunit association.

PubMed: 34285302
DOI: 10.1038/s41598-021-94236-y

実験手法

ELECTRON MICROSCOPY (3.5 Å)