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TitleA pseudoatomic model of the COPII cage obtained from cryo-electron microscopy and mass spectrometry.
Journal, issue, pagesNat Struct Mol Biol, Vol. 20, Issue 2, Page 167-173, Year 2013
Publish dateDec 23, 2012
AuthorsAlex J Noble / Qian Zhang / Jason O'Donnell / Hanaa Hariri / Nilakshee Bhattacharya / Alan G Marshall / Scott M Stagg /
PubMed AbstractCOPII 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 ...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-Å 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.
External linksNat Struct Mol Biol / PubMed:23262493 / PubMed Central
MethodsEM (single particle)
Resolution12.0 Å
Structure data

EMDB-5524:
A pseudoatomic model of the COPII cage obtained from cryo-electron microscopy and mass spectrometry
Method: EM (single particle) / Resolution: 12.0 Å

Source
  • Homo sapiens (human)

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