8TYM

Cryo-EM of the GDP-bound human dynamin (full-length) polymer assembled on the membrane in the super constricted state

8TYM の概要

• エントリーDOI: 10.2210/pdb8tym/pdb
• EMDBエントリー: 40942
• 分子名称: Dynamin-1, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: dynamin, membrane, fission, lipid, tubule, scission, endocytosis, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 346319.59

構造登録者

Jimah, J.R.,Canagarajah, B.J.,Hinshaw, J.E. (登録日: 2023-08-25, 公開日: 2024-06-12, 最終更新日: 2025-05-21)

主引用文献

Jimah, J.R.,Kundu, N.,Stanton, A.E.,Sochacki, K.A.,Canagarajah, B.,Chan, L.,Strub, M.P.,Wang, H.,Taraska, J.W.,Hinshaw, J.E.
Cryo-EM structures of membrane-bound dynamin in a post-hydrolysis state primed for membrane fission.
Dev.Cell, 59:1783-, 2024

PubMed Abstract: Dynamin assembles as a helical polymer at the neck of budding endocytic vesicles, constricting the underlying membrane as it progresses through the GTPase cycle to sever vesicles from the plasma membrane. Although atomic models of the dynamin helical polymer bound to guanosine triphosphate (GTP) analogs define earlier stages of membrane constriction, there are no atomic models of the assembled state post-GTP hydrolysis. Here, we used cryo-EM methods to determine atomic structures of the dynamin helical polymer assembled on lipid tubules, akin to necks of budding endocytic vesicles, in a guanosine diphosphate (GDP)-bound, super-constricted state. In this state, dynamin is assembled as a 2-start helix with an inner lumen of 3.4 nm, primed for spontaneous fission. Additionally, by cryo-electron tomography, we trapped dynamin helical assemblies within HeLa cells using the GTPase-defective dynamin K44A mutant and observed diverse dynamin helices, demonstrating that dynamin can accommodate a range of assembled complexes in cells that likely precede membrane fission.

PubMed: 38663399
DOI: 10.1016/j.devcel.2024.04.008

実験手法

ELECTRON MICROSCOPY (3.58 Å)