Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 20, Issue 2, Pages 167-173Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2467
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Funding
- US National Institutes of Health [R01GM086892]
- American Heart Association [0835300N]
- US National Science Foundation Division of Materials Research [DMR-06-54118]
- State of Florida
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COPII vesicles transport proteins from the endoplasmic reticulum to the Golgi apparatus. Previous COPII-cage cryo-EM structures lacked the resolution necessary to determine the residues of Sec13 and Sec31 that mediate assembly and flexibility of the COPII cage. Here we present a 12-angstrom structure of the human COPII cage, where the tertiary structure of Sec13 and Sec31 is clearly identifiable. We employ this structure and a homology model of the Sec13-Sec31 complex to create a reliable pseudoatomic model of the COPII cage. We combined this model with hydrogen/deuterium-exchange MS analysis to characterize four distinct contact regions at the vertices of the COPII cage. Furthermore, we found that the two-fold symmetry of the Sec31 dimeric region in Sec13-Sec31 is broken upon cage formation and that the resulting hinge is essential to form the proper edge geometry in COPII cages.
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