Structure of the Sec23/24–Sar1 pre-budding complex of the COPII vesicle coat View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-09

AUTHORS

Xiping Bi, Richard A. Corpina, Jonathan Goldberg

ABSTRACT

COPII-coated vesicles form on the endoplasmic reticulum by the stepwise recruitment of three cytosolic components: Sar1–GTP to initiate coat formation, Sec23/24 heterodimer to select SNARE and cargo molecules, and Sec13/31 to induce coat polymerization and membrane deformation. Crystallographic analysis of the Saccharomyces cerevisiae Sec23/24–Sar1 complex reveals a bow-tie-shaped structure, 15 nm long, with a membrane-proximal surface that is concave and positively charged to conform to the size and acidic-phospholipid composition of the COPII vesicle. Sec23 and Sar1 form a continuous surface stabilized by a non-hydrolysable GTP analogue, and Sar1 has rearranged from the GDP conformation to expose amino-terminal residues that will probably embed in the bilayer. The GTPase-activating protein (GAP) activity of Sec23 involves an arginine side chain inserted into the Sar1 active site. These observations establish the structural basis for GTP-dependent recruitment of a vesicular coat complex, and for uncoating through coat-controlled GTP hydrolysis. More... »

PAGES

271-277

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature01040

DOI

http://dx.doi.org/10.1038/nature01040

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1001233428

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12239560


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