4NXT

Crystal structure of the cytosolic domain of human MiD51

4NXT の概要

• エントリーDOI: 10.2210/pdb4nxt/pdb
• 関連するPDBエントリー: 4NXU 4NXV 4NXW 4NXX
• 分子名称: Mitochondrial dynamic protein MID51, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: nucleotidyltransferase, protein-protein interaction, adp, gdp, mitochondrial fission, mitochondria, membrane-anchored, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion outer membrane; Single-pass membrane protein: Q9NQG6
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 156499.75

構造登録者

Richter, V.,Ryan, M.T.,Kvansakul, M. (登録日: 2013-12-09, 公開日: 2013-12-25, 最終更新日: 2024-02-28)

主引用文献

Richter, V.,Palmer, C.S.,Osellame, L.D.,Singh, A.P.,Elgass, K.,Stroud, D.A.,Sesaki, H.,Kvansakul, M.,Ryan, M.T.
Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission.
J.Cell Biol., 204:477-486, 2014

PubMed Abstract: Mitochondrial fission is important for organelle transport, inheritance, and turnover, and alterations in fission are seen in neurological disease. In mammals, mitochondrial fission is executed by dynamin-related protein 1 (Drp1), a cytosolic guanosine triphosphatase that polymerizes and constricts the organelle. Recruitment of Drp1 to mitochondria involves receptors including Mff, MiD49, and MiD51. MiD49/51 form foci at mitochondrial constriction sites and coassemble with Drp1 to drive fission. Here, we solved the crystal structure of the cytosolic domain of human MiD51, which adopts a nucleotidyltransferase fold. Although MiD51 lacks catalytic residues for transferase activity, it specifically binds guanosine diphosphate and adenosine diphosphate. MiD51 mutants unable to bind nucleotides were still able to recruit Drp1. Disruption of an additional region in MiD51 that is not part of the nucleotidyltransferase fold blocked Drp1 recruitment and assembly of MiD51 into foci. MiD51 foci are also dependent on the presence of Drp1, and after scission they are distributed to daughter organelles, supporting the involvement of MiD51 in the fission apparatus.

PubMed: 24515348
DOI: 10.1083/jcb.201311014

実験手法

X-RAY DIFFRACTION (2.12 Å)