1m2v
From Proteopedia
(New page: 200px<br /><applet load="1m2v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m2v, resolution 2.75Å" /> '''Crystal Structure of...) |
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| - | [[Image:1m2v.gif|left|200px]]<br /><applet load="1m2v" size=" | + | [[Image:1m2v.gif|left|200px]]<br /><applet load="1m2v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m2v, resolution 2.75Å" /> | caption="1m2v, resolution 2.75Å" /> | ||
'''Crystal Structure of the yeast Sec23/24 heterodimer'''<br /> | '''Crystal Structure of the yeast Sec23/24 heterodimer'''<br /> | ||
==Overview== | ==Overview== | ||
| - | COPII-coated vesicles form on the endoplasmic reticulum by the stepwise | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1M2V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1M2V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Bi, X.]] | [[Category: Bi, X.]] | ||
| - | [[Category: Corpina, R | + | [[Category: Corpina, R A.]] |
[[Category: Goldberg, J.]] | [[Category: Goldberg, J.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:53 2008'' |
Revision as of 11:50, 21 February 2008
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Crystal Structure of the yeast Sec23/24 heterodimer
Overview
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.
About this Structure
1M2V is a Protein complex structure of sequences from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat., Bi X, Corpina RA, Goldberg J, Nature. 2002 Sep 19;419(6904):271-7. PMID:12239560
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