1m2v: Difference between revisions

Revision as of 23:06, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1m2v.png

Template:STRUCTURE 1m2v

Crystal Structure of the yeast Sec23/24 heterodimerCrystal Structure of the yeast Sec23/24 heterodimer

Template:ABSTRACT PUBMED 12239560

About this StructureAbout this Structure

1M2V is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Wed Jul 2 23:06:00 2008

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OCA

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-[[Image:1m2v.gif|left|200px]]
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 {{STRUCTURE_1m2v|  PDB=1m2v  |  SCENE=  }}
-'''Crystal Structure of the yeast Sec23/24 heterodimer'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12239560}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12239560}}
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 [[Category: Vwa domain]]
 [[Category: Zinc-finger]]
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