Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7MP8

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

Summary for 7MP8
Entry DOI10.2210/pdb7mp8/pdb
DescriptorSerine/threonine-protein kinase PINK1, mitochondrial-like Protein, SULFATE ION (3 entities in total)
Functional Keywordskinase, transphorylation, signaling protein
Biological sourceTribolium castaneum (Red flour beetle)
Total number of polymer chains1
Total formula weight51300.51
Authors
Rasool, S.,Veyron, S.,Trempe, J.F. (deposition date: 2021-05-04, release date: 2021-12-01, Last modification date: 2023-10-18)
Primary citationRasool, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

236371

PDB entries from 2025-05-21

PDB statisticsPDBj update infoContact PDBjnumon