7MP8

Crystal structure of the cytosolic domain of Tribolium castaneum PINK1 in the non-phosphorylated state

7MP8 の概要

• エントリーDOI: 10.2210/pdb7mp8/pdb
• 分子名称: Serine/threonine-protein kinase PINK1, mitochondrial-like Protein, SULFATE ION (3 entities in total)
• 機能のキーワード: kinase, transphorylation, signaling protein
• 由来する生物種: Tribolium castaneum (Red flour beetle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51300.51

構造登録者

Rasool, S.,Veyron, S.,Trempe, J.F. (登録日: 2021-05-04, 公開日: 2021-12-01, 最終更新日: 2023-10-18)

主引用文献

Rasool, S.,Veyron, S.,Soya, N.,Eldeeb, M.A.,Lukacs, G.L.,Fon, E.A.,Trempe, J.F.
Mechanism of PINK1 activation by autophosphorylation and insights into assembly on the TOM complex.
Mol.Cell, 82:44-, 2022

PubMed Abstract: Mutations in PINK1 cause autosomal-recessive Parkinson's disease. Mitochondrial damage results in PINK1 import arrest on the translocase of the outer mitochondrial membrane (TOM) complex, resulting in the activation of its ubiquitin kinase activity by autophosphorylation and initiation of Parkin-dependent mitochondrial clearance. Herein, we report crystal structures of the entire cytosolic domain of insect PINK1. Our structures reveal a dimeric autophosphorylation complex targeting phosphorylation at the invariant Ser205 (human Ser228). The dimer interface requires insert 2, which is unique to PINK1. The structures also reveal how an N-terminal helix binds to the C-terminal extension and provide insights into stabilization of PINK1 on the core TOM complex.

PubMed: 34875213
DOI: 10.1016/j.molcel.2021.11.012

実験手法

X-RAY DIFFRACTION (3 Å)