1m2o

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(New page: 200px<br /><applet load="1m2o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m2o, resolution 2.50&Aring;" /> '''Crystal Structure of...)
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[[Image:1m2o.gif|left|200px]]<br /><applet load="1m2o" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1m2o.gif|left|200px]]<br /><applet load="1m2o" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1m2o, resolution 2.50&Aring;" />
caption="1m2o, resolution 2.50&Aring;" />
'''Crystal Structure of the Sec23-Sar1 complex'''<br />
'''Crystal Structure of the Sec23-Sar1 complex'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1M2O 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, MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M2O OCA].
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1M2O 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>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GNP:'>GNP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2O OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Bi, X.]]
[[Category: Bi, X.]]
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[[Category: Corpina, R.A.]]
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[[Category: Corpina, R A.]]
[[Category: Goldberg, J.]]
[[Category: Goldberg, J.]]
[[Category: GNP]]
[[Category: GNP]]
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[[Category: zinc-finger]]
[[Category: zinc-finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:05:47 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:54 2008''

Revision as of 11:51, 21 February 2008

Image:1m2o.gif

1m2o, resolution 2.50Å

Drag the structure with the mouse to rotate

Crystal Structure of the Sec23-Sar1 complex

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

1M2O is a Protein complex structure of sequences from Saccharomyces cerevisiae with , and as ligands. 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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