3ZYC

DYNAMIN 1 GTPASE GED FUSION DIMER COMPLEXED WITH GMPPCP

3ZYC の概要

• エントリーDOI: 10.2210/pdb3zyc/pdb
• 関連するPDBエントリー: 1DYN 2DYN 2X2E 2X2F
• 分子名称: DYNAMIN-1, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, membrane fission, nucleotide-binding, endocytosis, motor protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79868.95

構造登録者

Chappie, J.S.,Mears, J.A.,Fang, S.,Leonard, M.,Schmid, S.L.,Milligan, R.A.,Hinshaw, J.E.,Dyda, F. (登録日: 2011-08-22, 公開日: 2011-10-12, 最終更新日: 2023-12-20)

主引用文献

Chappie, J.S.,Mears, J.A.,Fang, S.,Leonard, M.,Schmid, S.L.,Milligan, R.A.,Hinshaw, J.E.,Dyda, F.
A Pseudoatomic Model of the Dynamin Polymer Identifies a Hydrolysis-Dependent Powerstroke.
Cell(Cambridge,Mass.), 147:209-, 2011

PubMed Abstract: The GTPase dynamin catalyzes membrane fission by forming a collar around the necks of clathrin-coated pits, but the specific structural interactions and conformational changes that drive this process remain a mystery. We present the GMPPCP-bound structures of the truncated human dynamin 1 helical polymer at 12.2 Å and a fusion protein, GG, linking human dynamin 1's catalytic G domain to its GTPase effector domain (GED) at 2.2 Å. The structures reveal the position and connectivity of dynamin fragments in the assembled structure, showing that G domain dimers only form between tetramers in sequential rungs of the dynamin helix. Using chemical crosslinking, we demonstrate that dynamin tetramers are made of two dimers, in which the G domain of one molecule interacts in trans with the GED of another. Structural comparison of GG(GMPPCP) to the GG transition-state complex identifies a hydrolysis-dependent powerstroke that may play a role in membrane-remodeling events necessary for fission.

PubMed: 21962517
DOI: 10.1016/J.CELL.2011.09.003

実験手法

X-RAY DIFFRACTION (2.2 Å)