7PV1

Crystal structure of the dimeric mitofilin domain of Mic60 in complex with the CHCH domain of Mic19

7PV1 の概要

• エントリーDOI: 10.2210/pdb7pv1/pdb
• 関連するPDBエントリー: 7PUZ 7PV0
• 分子名称: MICOS complex subunit MIC60 fused to MIC19, TETRAETHYLENE GLYCOL (3 entities in total)
• 機能のキーワード: micos, dimer, mitochondria, fusion protein, structural protein
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68903.98

構造登録者

Funck, K.,Bock-Bierbaum, T.,Daumke, O. (登録日: 2021-10-01, 公開日: 2022-09-07, 最終更新日: 2024-11-13)

主引用文献

Bock-Bierbaum, T.,Funck, K.,Wollweber, F.,Lisicki, E.,von der Malsburg, K.,von der Malsburg, A.,Laborenz, J.,Noel, J.K.,Hessenberger, M.,Jungbluth, S.,Bernert, C.,Kunz, S.,Riedel, D.,Lilie, H.,Jakobs, S.,van der Laan, M.,Daumke, O.
Structural insights into crista junction formation by the Mic60-Mic19 complex.
Sci Adv, 8:eabo4946-eabo4946, 2022

PubMed Abstract: Mitochondrial cristae membranes are the oxidative phosphorylation sites in cells. Crista junctions (CJs) form the highly curved neck regions of cristae and are thought to function as selective entry gates into the cristae space. Little is known about how CJs are generated and maintained. We show that the central coiled-coil (CC) domain of the mitochondrial contact site and cristae organizing system subunit Mic60 forms an elongated, bow tie-shaped tetrameric assembly. Mic19 promotes Mic60 tetramerization via a conserved interface between the Mic60 mitofilin and Mic19 CHCH (CC-helix-CC-helix) domains. Dimerization of mitofilin domains exposes a crescent-shaped membrane-binding site with convex curvature tailored to interact with the curved CJ neck. Our study suggests that the Mic60-Mic19 subcomplex traverses CJs as a molecular strut, thereby controlling CJ architecture and function.

PubMed: 36044574
DOI: 10.1126/sciadv.abo4946

実験手法

X-RAY DIFFRACTION (2.497 Å)