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The GTPase dynamin is essential for numerous vesiculation events including clathrin-mediated endocytosis. Upon GTP hydrolysis, dynamin constricts a lipid bilayer. Previously, a three-dimensional structure of mutant dynamin in the constricted state was determined by helical reconstruction methods. We solved the nonconstricted state by a single-particle approach and show that the stalk region of dynamin undergoes a large conformational change that drives tube constriction.

Original publication

DOI

10.1038/nsmb762

Type

Journal article

Journal

Nat Struct Mol Biol

Publication Date

06/2004

Volume

11

Pages

574 - 575

Keywords

Dynamins, Lipid Bilayers, Microscopy, Electron, Molecular Motor Proteins, Protein Conformation