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Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin

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A dynamin mutant defines a superconstricted prefission state.

Anna C Sundborger¹, Shunming Fang¹, Jürgen A Heymann¹

¹Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

|August 5, 2014

Summary

Dynamin

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Area of Science:

Molecular and Cell Biology
Biophysics

Background:

Dynamin is a GTPase essential for endocytosis.
Its oligomeric assembly and GTP hydrolysis drive membrane fission.
The transition state of GTP hydrolysis is critical for fission efficiency.

Purpose of the Study:

To determine the structure of a dynamin mutant (K44A) in a prefission state.
To elucidate the mechanism of dynamin-mediated membrane fission.

Main Methods:

X-ray crystallography at 12.5 Å resolution.
Computational docking and modeling.

Main Results:

A superconstricted dynamin structure (3.7 nm diameter) was resolved, reaching the fission limit.
The ground-state conformation and two-start helical symmetry facilitate efficient tetramer packing.
A model for the minimal dynamin fission machine was proposed.

Conclusions:

Dynamin's assembly and GTPase activity are finely tuned for membrane fission.
The study provides structural insights into the dynamin fission mechanism.