A pseudoatomic model of the dynamin polymer identifies a hydrolysis-dependent powerstroke

Joshua S. Chappie, Jason A. Mears, Shunming Fang, Marilyn Leonard, Sandra L. Schmid, Ronald A. Milligan, Jenny E. Hinshaw, Fred Dyda

Research output: Contribution to journalArticlepeer-review

164 Scopus citations


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 and a fusion protein, GG, linking human dynamin 1's catalytic G domain to its GTPase effector domain (GED) at 2.2 . 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 GGGMPPCP to the GG transition-state complex identifies a hydrolysis-dependent powerstroke that may play a role in membrane-remodeling events necessary for fission.

Original languageEnglish (US)
Pages (from-to)209-222
Number of pages14
Issue number1
StatePublished - Sep 30 2011

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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