4BZI

The structure of the COPII coat assembled on membranes

Summary for 4BZI

• Entry DOI: 10.2210/pdb4bzi/pdb
• Related: 4BZJ 4BZK
• EMDB information: 2428 2430 2431
• Descriptor: SEC23P, SAR1P, SEC24P, ... (7 entities in total)
• Functional Keywords: transport protein, secretion, trafficking, sec23, sec24, sar1
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Total number of polymer chains: 12
• Total formula weight: 945064.64

Authors

Zanetti, G.,Prinz, S.,Daum, S.,Meister, A.,Schekman, R.,Bacia, K.,Briggs, J.A.G. (deposition date: 2013-07-26, release date: 2013-09-18, Last modification date: 2024-05-08)

Primary citation

Zanetti, G.,Prinz, S.,Daum, S.,Meister, A.,Schekman, R.,Bacia, K.,Briggs, J.A.G.
The Structure of the Copii Transport-Vesicle Coat Assembled on Membranes
Elife, 2:00951-, 2013

PubMed Abstract: Coat protein complex II (COPII) mediates formation of the membrane vesicles that export newly synthesised proteins from the endoplasmic reticulum. The inner COPII proteins bind to cargo and membrane, linking them to the outer COPII components that form a cage around the vesicle. Regulated flexibility in coat architecture is essential for transport of a variety of differently sized cargoes, but structural data on the assembled coat has not been available. We have used cryo-electron tomography and subtomogram averaging to determine the structure of the complete, membrane-assembled COPII coat. We describe a novel arrangement of the outer coat and find that the inner coat can assemble into regular lattices. The data reveal how coat subunits interact with one another and with the membrane, suggesting how coordinated assembly of inner and outer coats can mediate and regulate packaging of vesicles ranging from small spheres to large tubular carriers. DOI:http://dx.doi.org/10.7554/eLife.00951.001.

PubMed: 24062940
DOI: 10.7554/ELIFE.00951

Experimental method

ELECTRON MICROSCOPY (23 Å)