4L9O

Crystal Structure of the Sec13-Sec16 blade-inserted complex from Pichia pastoris

Summary for 4L9O

• Entry DOI: 10.2210/pdb4l9o/pdb
• Descriptor: Sec16,Protein transport protein SEC13, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: beta propeller, copii, vesicle coat budding, nuclear pore complex proteins, cop-coated vesicles, endoplasmic reticulum, ace1, protein transport
• Biological source: Komagataella pastoris (Yeast); More
• Cellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : P53024
• Total number of polymer chains: 2
• Total formula weight: 77471.75

Authors

McMahon, C.,Jeffrey, P.D.,Hughson, F.M. (deposition date: 2013-06-18, release date: 2013-10-02, Last modification date: 2023-09-20)

Primary citation

Bharucha, N.,Liu, Y.,Papanikou, E.,McMahon, C.,Esaki, M.,Jeffrey, P.D.,Hughson, F.M.,Glick, B.S.
Sec16 influences transitional ER sites by regulating rather than organizing COPII.
Mol Biol Cell, 24:3406-3419, 2013

PubMed Abstract: During the budding of coat protein complex II (COPII) vesicles from transitional endoplasmic reticulum (tER) sites, Sec16 has been proposed to play two distinct roles: negatively regulating COPII turnover and organizing COPII assembly at tER sites. We tested these ideas using the yeast Pichia pastoris. Redistribution of Sec16 to the cytosol accelerates tER dynamics, supporting a negative regulatory role for Sec16. To evaluate a possible COPII organization role, we dissected the functional regions of Sec16. The central conserved domain, which had been implicated in coordinating COPII assembly, is actually dispensable for normal tER structure. An upstream conserved region (UCR) localizes Sec16 to tER sites. The UCR binds COPII components, and removal of COPII from tER sites also removes Sec16, indicating that COPII recruits Sec16 rather than the other way around. We propose that Sec16 does not in fact organize COPII. Instead, regulation of COPII turnover can account for the influence of Sec16 on tER sites.

PubMed: 24006484
DOI: 10.1091/mbc.E13-04-0185

Experimental method

X-RAY DIFFRACTION (1.6 Å)