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Related Experiment Video

Updated: May 14, 2026

Origami Inspired Self-assembly of Patterned and Reconfigurable Particles

Origami Inspired Self-assembly of Patterned and Reconfigurable Particles

Published on: February 4, 2013

The exomer cargo adaptor features a flexible hinge domain.

Brian C Richardson¹, J Christopher Fromme

¹Department of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853, USA.

Structure (London, England : 1993)

|February 12, 2013

Summary

Exomer, a protein complex, uses a flexible hinge to bind cargo and membranes during vesicle formation. This flexibility helps maintain interactions on dynamic, curved cellular membranes.

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Area of Science:

Cell biology
Structural biology
Protein-protein interactions

Background:

Exomer functions as a cargo adaptor, mediating protein sorting into vesicles at the trans-Golgi network.
Cargo adaptors must interact with cargo, regulatory proteins, and the membrane surface.
Membrane curvature changes during vesicle biogenesis, challenging adaptor interactions.

Purpose of the Study:

To elucidate the structural basis of exomer function in dynamic membrane environments.
To investigate the flexibility of the tetrameric Chs5/Bch1 exomer complex.

Main Methods:

X-ray crystallography to determine the structure of the Chs5/Bch1 exomer complex.
Small-angle X-ray scattering (SAXS) to assess complex flexibility in solution.

Main Results:

The crystal structure of a tetrameric Chs5/Bch1 exomer complex was determined.
SAXS data demonstrated significant flexibility of the exomer complex in solution.
Structural analysis revealed flexibility centered around the dimeric N-terminal domain of Chs5 subunits.

Conclusions:

The exomer complex possesses a flexible hinge mechanism, primarily involving the Chs5 N-terminal domain.
This flexibility is proposed to be crucial for maintaining protein-protein and protein-membrane interactions during vesicle formation on changing membrane surfaces.