Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat
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Schwartz_Structure of the.pdf
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13 MB
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Author(s)
Schwartz, Thomas
Whittle, James Richardson Ross
Date Issued
August 2010
Journal
The Journal of Cell Biology
Publisher
Rockefeller University Press
Citation
Whittle, J. R. R., and T. U. Schwartz. “Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat.” The Journal of Cell Biology 190, no. 3 (August 9, 2010): 347-361.
Version
Final published version
Abstract
Ancestral coatomer element 1 (ACE1) proteins assemble latticework coats for COPII vesicles and the nuclear pore complex. The ACE1 protein Sec31 and Sec13 make a 2:2 tetramer that forms the edge element of the COPII outer coat. In this study, we report that the COPII accessory protein Sec16 also contains an ACE1. The 165-kD crystal structure of the central domain of Sec16 in complex with Sec13 was solved at 2.7-Å resolution. Sec16 and Sec13 also make a 2:2 tetramer, another edge element for the COPII system. Domain swapping at the ACE1–ACE1 interface is observed both in the prior structure of Sec13–Sec31 and in Sec13–Sec16. A Sec31 mutant in which domain swapping is prevented adopts an unprecedented laminated structure, solved at 2.8-Å resolution. Our in vivo data suggest that the ACE1 element of Sec31 can functionally replace the ACE1 element of Sec16. Our data support Sec16 as a scaffold for the COPII system and a template for the Sec13–Sec31 coat.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1083/jcb.201003092
