3MZK

Sec13/Sec16 complex, S.cerevisiae

Summary for 3MZK

• Entry DOI: 10.2210/pdb3mzk/pdb
• Related: 3MZL
• Descriptor: Protein transport protein SEC13, Protein transport protein SEC16 (3 entities in total)
• Functional Keywords: alpha-helical-stack, beta-propeller, protein transport
• Biological source: Saccharomyces cerevisiae (yeast); More
• Cellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side: Q04491; Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side: P48415
• Total number of polymer chains: 4
• Total formula weight: 165976.09

Authors

Whittle, J.R.,Schwartz, T.U. (deposition date: 2010-05-12, release date: 2010-08-18, Last modification date: 2024-04-03)

Primary citation

Whittle, J.R.,Schwartz, T.U.
Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat.
J.Cell Biol., 190:347-361, 2010

PubMed 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-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.

PubMed: 20696705
DOI: 10.1083/jcb.201003092

Experimental method

X-RAY DIFFRACTION (2.69 Å)