4UUD

Human dynamin 1 K44A superconstricted polymer stabilized with GTP

4UUD の概要

• エントリーDOI: 10.2210/pdb4uud/pdb
• 関連するPDBエントリー: 4UUK
• EMDBエントリー: 2701
• 分子名称: DYNAMIN-1 (2 entities in total)
• 機能のキーワード: structural protein, dynamin, endocytosis, membrane fission, gtpase, intracellular trafficking, hydrolysis, superconstriction
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cytoplasm : Q05193 Q05193
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 1170444.19

構造登録者

Sundborger, A.C.,Fang, S.,Heymann, J.A.,Ray, P.,Chappie, J.S.,Hinshaw, J.E. (登録日: 2014-07-25, 公開日: 2014-08-27, 最終更新日: 2024-05-08)

主引用文献

Sundborger, A.C.,Fang, S.,Heymann, J.A.,Ray, P.,Chappie, J.S.,Hinshaw, J.E.
A Dynamin Mutant Defines a Superconstricted Prefission State.
Cell Rep., 8:734-, 2014

PubMed Abstract: Dynamin is a 100 kDa GTPase that organizes into helical assemblies at the base of nascent clathrin-coated vesicles. Formation of these oligomers stimulates the intrinsic GTPase activity of dynamin, which is necessary for efficient membrane fission during endocytosis. Recent evidence suggests that the transition state of dynamin's GTP hydrolysis reaction serves as a key determinant of productive fission. Here, we present the structure of a transition-state-defective dynamin mutant K44A trapped in a prefission state at 12.5 Å resolution. This structure constricts to 3.7 nm, reaching the theoretical limit required for spontaneous membrane fission. Computational docking indicates that the ground-state conformation of the dynamin polymer is sufficient to achieve this superconstricted prefission state and reveals how a two-start helical symmetry promotes the most efficient packing of dynamin tetramers around the membrane neck. These data suggest a model for the assembly and regulation of the minimal dynamin fission machine.

PubMed: 25088425
DOI: 10.1016/J.CELREP.2014.06.054

実験手法

ELECTRON MICROSCOPY (12.5 Å)