The crystal structure of dynamin

Nature. 2011 Sep 18;477(7366):561-6. doi: 10.1038/nature10441.


Dynamin-related proteins (DRPs) are multi-domain GTPases that function via oligomerization and GTP-dependent conformational changes to play central roles in regulating membrane structure across phylogenetic kingdoms. How DRPs harness self-assembly and GTP-dependent conformational changes to remodel membranes is not understood. Here we present the crystal structure of an assembly-deficient mammalian endocytic DRP, dynamin 1, lacking the proline-rich domain, in its nucleotide-free state. The dynamin 1 monomer is an extended structure with the GTPase domain and bundle signalling element positioned on top of a long helical stalk with the pleckstrin homology domain flexibly attached on its opposing end. Dynamin 1 dimer and higher order dimer multimers form via interfaces located in the stalk. Analysis of these interfaces provides insight into DRP family member specificity and regulation and provides a framework for understanding the biogenesis of higher order DRP structures and the mechanism of DRP-mediated membrane scission events.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Dynamin I / chemistry*
  • Dynamin I / genetics
  • Dynamin I / metabolism
  • Guanosine Triphosphate / metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleotides
  • Protein Binding
  • Protein Conformation
  • Protein Multimerization / genetics
  • Protein Structure, Tertiary / genetics
  • Rats


  • Nucleotides
  • Guanosine Triphosphate
  • Dynamin I

Associated data

  • PDB/3ZVR