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2j3r
From Proteopedia
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| - | [[Image:2j3r.gif|left|200px]]<br /> | ||
| - | <applet load="2j3r" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2j3r, resolution 2.6Å" /> | ||
| - | '''THE CRYSTAL STRUCTURE OF THE BET3-TRS31 HETERODIMER.'''<br /> | ||
| - | == | + | ==The crystal structure of the bet3-trs31 heterodimer.== |
| - | Transport protein particle (TRAPP) I is a multisubunit vesicle tethering | + | <StructureSection load='2j3r' size='340' side='right'caption='[[2j3r]], [[Resolution|resolution]] 2.60Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2j3r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J3R FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1vpg|1vpg]], [[1wc8|1wc8]], [[1wc9|1wc9]], [[2j3t|2j3t]], [[2j3w|2j3w]]</div></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=2j3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j3r OCA], [https://pdbe.org/2j3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j3r RCSB], [https://www.ebi.ac.uk/pdbsum/2j3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j3r ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/j3/2j3r_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=2j3r ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Transport protein particle (TRAPP) I is a multisubunit vesicle tethering factor composed of seven subunits involved in ER-to-Golgi trafficking. The functional mechanism of the complex and how the subunits interact to form a functional unit are unknown. Here, we have used a multidisciplinary approach that includes X-ray crystallography, electron microscopy, biochemistry, and yeast genetics to elucidate the architecture of TRAPP I. The complex is organized through lateral juxtaposition of the subunits into a flat and elongated particle. We have also localized the site of guanine nucleotide exchange activity to a highly conserved surface encompassing several subunits. We propose that TRAPP I attaches to Golgi membranes with its large flat surface containing many highly conserved residues and forms a platform for protein-protein interactions. This study provides the most comprehensive view of a multisubunit vesicle tethering complex to date, based on which a model for the function of this complex, involving Rab1-GTP and long, coiled-coil tethers, is presented. | ||
| - | + | The architecture of the multisubunit TRAPP I complex suggests a model for vesicle tethering.,Kim YG, Raunser S, Munger C, Wagner J, Song YL, Cygler M, Walz T, Oh BH, Sacher M Cell. 2006 Nov 17;127(4):817-30. PMID:17110339<ref>PMID:17110339</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2j3r" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Kim, Y | + | __TOC__ |
| - | [[Category: Oh, B | + | </StructureSection> |
| - | + | [[Category: Brachidanio rerio]] | |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Lk3 transgenic mice]] |
| - | [[Category: | + | [[Category: Kim, Y G]] |
| - | [[Category: | + | [[Category: Oh, B H]] |
| - | [[Category: | + | [[Category: Endoplasmic reticulum]] |
| - | [[Category: | + | [[Category: Er-golgi transport]] |
| - | [[Category: | + | [[Category: Golgi apparatus]] |
| - | [[Category: | + | [[Category: Lipoprotein]] |
| - | [[Category: | + | [[Category: Multisubunit tethering factor]] |
| - | + | [[Category: Palmitate]] | |
| - | + | [[Category: Transport]] | |
| + | [[Category: Trapp]] | ||
| + | [[Category: Vesicle transport]] | ||
Current revision
The crystal structure of the bet3-trs31 heterodimer.
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