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| {{STRUCTURE_1m2v| PDB=1m2v | SCENE= }} | | {{STRUCTURE_1m2v| PDB=1m2v | SCENE= }} |
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| '''Crystal Structure of the yeast Sec23/24 heterodimer'''
| | ===Crystal Structure of the yeast Sec23/24 heterodimer=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12239560}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12239560 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12239560}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Vwa domain]] | | [[Category: Vwa domain]] |
| [[Category: Zinc-finger]] | | [[Category: Zinc-finger]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:34:00 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:06:00 2008'' |