Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat.

Publication Type:

Journal Article

Authors:

Whittle, James R R; Schwartz, Thomas U

Source:

J Cell Biol, Volume 190, Issue 3, p.347-61 (2010)

Keywords:

COP-Coated Vesicles, DNA-Binding Proteins, Endoplasmic Reticulum, Membrane Proteins, Models, Molecular, Mutation, Nuclear Pore Complex Proteins, Protein Structure, Secondary, Saccharomyces cerevisiae Proteins, Transcription Factors

Abstract:

<p>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-A 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-A 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.</p>