6FGZ

Cyanidioschyzon merolae Dnm1 (CmDnm1)

6FGZ の概要

• エントリーDOI: 10.2210/pdb6fgz/pdb
• 分子名称: Dynamin (1 entity in total)
• 機能のキーワード: dynamin, mitochondrial fission, lipid binding protein
• 由来する生物種: Cyanidioschyzon merolae (Red alga)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 87294.98

構造登録者

Bohuszewicz, O.,Low, H.H. (登録日: 2018-01-11, 公開日: 2018-08-15, 最終更新日: 2024-01-17)

主引用文献

Bohuszewicz, O.,Low, H.H.
Structure of a mitochondrial fission dynamin in the closed conformation.
Nat. Struct. Mol. Biol., 25:722-731, 2018

PubMed Abstract: Dynamin 1-like proteins (DNM1-L) are mechanochemical GTPases that induce membrane fission in mitochondria and peroxisomes. Their mechanism depends on conformational changes driven by nucleotide and lipid cycling. Here we show the crystal structure of a mitochondrial fission dynamin (CmDnm1) from the algae Cyanidioschyzon merolae. Unlike other eukaryotic dynamin structures, CmDnm1 is in a hinge 1 closed conformation, with the GTPase domain compacted against the stalk. Within the crystal, CmDnm1 packs as a diamond-shaped tetramer that is consistent with an inactive off-membrane state. Crosslinking, photoinduced electron transfer assays, and electron microscopy verify these structures. In vitro, CmDnm1 forms concentration-dependent rings and protein-lipid tubes reminiscent of DNM1-L and classical dynamin with hinge 1 open. Our data provides a mechanism for filament collapse and membrane release that may extend to other dynamin family members. Additionally, hinge 1 closing may represent a key conformational change that contributes to membrane fission.

PubMed: 30061604
DOI: 10.1038/s41594-018-0097-6

実験手法

X-RAY DIFFRACTION (7.002 Å)