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[[Image:1m2o.gif|left|200px]]


{{Structure
==Crystal Structure of the Sec23-Sar1 complex==
|PDB= 1m2o |SIZE=350|CAPTION= <scene name='initialview01'>1m2o</scene>, resolution 2.50&Aring;
<StructureSection load='1m2o' size='340' side='right'caption='[[1m2o]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene>
<table><tr><td colspan='2'>[[1m2o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M2O FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|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])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m2o OCA], [https://pdbe.org/1m2o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m2o RCSB], [https://www.ebi.ac.uk/pdbsum/1m2o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m2o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SEC23_YEAST SEC23_YEAST] Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalisation of plasma membrane proteins like the maltose transporter.<ref>PMID:2670558</ref> <ref>PMID:6996832</ref> <ref>PMID:7026045</ref> <ref>PMID:3293799</ref> <ref>PMID:3049622</ref> <ref>PMID:2188733</ref> <ref>PMID:1498369</ref> <ref>PMID:7925484</ref> <ref>PMID:8451644</ref> <ref>PMID:8548805</ref> <ref>PMID:8909535</ref> <ref>PMID:9427388</ref> <ref>PMID:9023343</ref> <ref>PMID:9624457</ref> <ref>PMID:9428766</ref> <ref>PMID:10198022</ref> <ref>PMID:11086000</ref> <ref>PMID:10720463</ref> <ref>PMID:12941276</ref> <ref>PMID:14627716</ref> <ref>PMID:16269340</ref> <ref>PMID:17287728</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m2/1m2o_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m2o ConSurf].
<div style="clear:both"></div>


'''Crystal Structure of the Sec23-Sar1 complex'''
==See Also==
 
*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1M2O is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2O 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:[http://www.ncbi.nlm.nih.gov/pubmed/12239560 12239560]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Bi, X.]]
[[Category: Bi X]]
[[Category: Corpina, R A.]]
[[Category: Corpina RA]]
[[Category: Goldberg, J.]]
[[Category: Goldberg J]]
[[Category: GNP]]
[[Category: MG]]
[[Category: ZN]]
[[Category: beta barrel]]
[[Category: gelsolin domain]]
[[Category: vwa domain]]
[[Category: zinc-finger]]
 
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