Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat Journal Article
| Authors: | Bi, X.; Corpina, R. A.; Goldberg, J. |
| Article Title: | Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat |
| 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 bowtie-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. |
| Keywords: | nonhuman; protein binding; membrane proteins; endoplasmic reticulum; amino acid sequence; molecular sequence data; protein synthesis; saccharomyces cerevisiae; polymerization; recombinant protein; guanosine triphosphatase activating protein; binding site; models, molecular; dimerization; crystallography, x-ray; protein structure, tertiary; binding sites; yeast; saccharomyces cerevisiae proteins; crystallization; biochemistry; guanosine triphosphate; hydrolysis; protein structure, secondary; protein isoforms; biological transport; macromolecular substances; phospholipid; golgi complex; membrane vesicle; molecules; guanosine diphosphate; guanosine triphosphatase; monomeric gtp-binding proteins; cop-coated vesicles; vesicle; snare protein; vesicles; biological membranes; saccharomyces; natural sciences; priority journal; article |
| Journal Title: | Nature |
| Volume: | 419 |
| Issue: | 6904 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 2002-09-19 |
| Start Page: | 271 |
| End Page: | 277 |
| Language: | English |
| DOI: | 10.1038/nature01040 |
| PUBMED: | 12239560 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 14 November 2014 -- Source: Scopus |
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