1m2v: Difference between revisions

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[[Image:1m2v.gif|left|200px]]
[[Image:1m2v.gif|left|200px]]


{{Structure
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|SITE=
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|GENE= Sec23 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), Sar1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
{{STRUCTURE_1m2v| PDB=1m2v  | SCENE= }}  
|RELATEDENTRY=[[1m2o|1M2O]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m2v OCA], [http://www.ebi.ac.uk/pdbsum/1m2v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m2v RCSB]</span>
}}


'''Crystal Structure of the yeast Sec23/24 heterodimer'''
'''Crystal Structure of the yeast Sec23/24 heterodimer'''
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[[Category: Corpina, R A.]]
[[Category: Corpina, R A.]]
[[Category: Goldberg, J.]]
[[Category: Goldberg, J.]]
[[Category: beta barrel]]
[[Category: Beta barrel]]
[[Category: gelsolin domain,]]
[[Category: Gelsolin domain]]
[[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 Sun Mar 30 22:10:33 2008''

Revision as of 00:34, 3 May 2008

File:1m2v.gif

Template:STRUCTURE 1m2v

Crystal Structure of the yeast Sec23/24 heterodimer


OverviewOverview

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 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 Sat May 3 00:34:00 2008

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