7MP9

Crystal structure of the cytosolic domain of Tribolium castaneum PINK1 phosphorylated at Ser205 in complex with ADP analog

Summary for 7MP9

• Entry DOI: 10.2210/pdb7mp9/pdb
• Descriptor: Serine/threonine-protein kinase PINK1, mitochondrial-like Protein, MAGNESIUM ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: kinase, transphorylation, signaling protein
• Biological source: Tribolium castaneum (Red flour beetle)
• Total number of polymer chains: 1
• Total formula weight: 52685.80

Authors

Rasool, S.,Veyron, S.,Trempe, J.F. (deposition date: 2021-05-04, release date: 2021-12-01, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)