4OAF

Crystal structure of the cytosolic domain of mouse MiD51

4OAF の概要

• エントリーDOI: 10.2210/pdb4oaf/pdb
• 関連するPDBエントリー: 4OAG 4OAH 4OAI
• 分子名称: Mitochondrial dynamic protein MID51 (2 entities in total)
• 機能のキーワード: nucleotidyl transferase fold, transferase
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Mitochondrion outer membrane; Single-pass membrane protein (By similarity): Q8BGV8
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 149011.00

構造登録者

Loson, O.C.,Kaiser, J.T.,Chan, D.C. (登録日: 2014-01-04, 公開日: 2014-01-22, 最終更新日: 2024-02-28)

主引用文献

Loson, O.C.,Liu, R.,Rome, M.E.,Meng, S.,Kaiser, J.T.,Shan, S.O.,Chan, D.C.
The Mitochondrial Fission Receptor MiD51 Requires ADP as a Cofactor.
Structure, 22:367-377, 2014

PubMed Abstract: Mitochondrial fission requires recruitment of dynamin-related protein 1 (Drp1) to the mitochondrial surface and activation of its GTP-dependent scission function. The Drp1 receptors MiD49 and MiD51 recruit Drp1 to facilitate mitochondrial fission, but their mechanism of action is poorly understood. Using X-ray crystallography, we demonstrate that MiD51 contains a nucleotidyl transferase domain that binds ADP with high affinity. MiD51 recruits Drp1 via a surface loop that functions independently of ADP binding. However, in the absence of nucleotide binding, the recruited Drp1 cannot be activated for fission. Purified MiD51 strongly inhibits Drp1 assembly and GTP hydrolysis in the absence of ADP. Addition of ADP relieves this inhibition and promotes Drp1 assembly into spirals with enhanced GTP hydrolysis. Our results reveal ADP as an essential cofactor for MiD51 during mitochondrial fission.

PubMed: 24508339
DOI: 10.1016/j.str.2014.01.001

実験手法

X-RAY DIFFRACTION (2.2 Å)