1m2v: Difference between revisions

Revision as of 14:50, 21 February 2008

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 with as ligand. 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

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OCA

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-[[Image:1m2v.gif|left|200px]]<br /><applet load="1m2v" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1m2v.gif|left|200px]]<br /><applet load="1m2v" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1m2v, resolution 2.75&Aring;" />
 '''Crystal Structure of the yeast Sec23/24 heterodimer'''<br />
 ==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.
+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==
-M2V 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M2V OCA].
+M2V 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==
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 [[Category: Saccharomyces cerevisiae]]
 [[Category: Bi, X.]]
-[[Category: Corpina, R.A.]]
+[[Category: Corpina, R A.]]
 [[Category: Goldberg, J.]]
 [[Category: ZN]]
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 [[Category: zinc-finger]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:06:11 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:53 2008''