7AX3

CryoEM structure of the super-constricted two-start dynamin 1 filament

これはPDB形式変換不可エントリーです。

7AX3 の概要

• エントリーDOI: 10.2210/pdb7ax3/pdb
• EMDBエントリー: 11932
• 分子名称: Dynamin-1, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: dynamin, cytosolic protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 36
• 化学式量合計: 3530947.39

構造登録者

Liu, J.W.,Zhang, P.J. (登録日: 2020-11-09, 公開日: 2021-11-10, 最終更新日: 2025-10-01)

主引用文献

Liu, J.,Alvarez, F.J.D.,Clare, D.K.,Noel, J.K.,Zhang, P.
CryoEM structure of the super-constricted two-start dynamin 1 filament.
Nat Commun, 12:5393-5393, 2021

PubMed Abstract: Dynamin belongs to the large GTPase superfamily, and mediates the fission of vesicles during endocytosis. Dynamin molecules are recruited to the neck of budding vesicles to assemble into a helical collar and to constrict the underlying membrane. Two helical forms were observed: the one-start helix in the constricted state and the two-start helix in the super-constricted state. Here we report the cryoEM structure of a super-constricted two-start dynamin 1 filament at 3.74 Å resolution. The two strands are joined by the conserved GTPase dimeric interface. In comparison with the one-start structure, a rotation around Hinge 1 is observed, essential for communicating the chemical power of the GTPase domain and the mechanical force of the Stalk and PH domain onto the underlying membrane. The Stalk interfaces are well conserved and serve as fulcrums for adapting to changing curvatures. Relative to one-start, small rotations per interface accumulate to bring a drastic change in the helical pitch. Elasticity theory rationalizes the diversity of dynamin helical symmetries and suggests corresponding functional significance.

PubMed: 34518553
DOI: 10.1038/s41467-021-25741-x

実験手法

ELECTRON MICROSCOPY (3.74 Å)