3cue: Difference between revisions

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-{{Seed}}
-[[Image:3cue.png|left|200px]]
-<!--
+==Crystal structure of a TRAPP subassembly activating the Rab Ypt1p==
-The line below this paragraph, containing "STRUCTURE_3cue", creates the "Structure Box" on the page.
+<StructureSection load='3cue' size='340' side='right'caption='[[3cue]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3cue]] is a 24 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=3CUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CUE FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr>
-{{STRUCTURE_3cue|  PDB=3cue  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cue OCA], [https://pdbe.org/3cue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cue RCSB], [https://www.ebi.ac.uk/pdbsum/3cue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cue ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRS23_YEAST TRS23_YEAST] Component of the TRAPP I, TRAPP II and TRAPP III complexes which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation.<ref>PMID:11239471</ref> <ref>PMID:20972447</ref> <ref>PMID:20375281</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/cu/3cue_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3cue ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The multimeric membrane-tethering complexes TRAPPI and TRAPPII share seven subunits, of which four (Bet3p, Bet5p, Trs23p, and Trs31p) are minimally needed to activate the Rab GTPase Ypt1p in an event preceding membrane fusion. Here, we present the structure of a heteropentameric TRAPPI assembly complexed with Ypt1p. We propose that TRAPPI facilitates nucleotide exchange primarily by stabilizing the nucleotide-binding pocket of Ypt1p in an open, solvent-accessible form. Bet3p, Bet5p, and Trs23p interact directly with Ypt1p to stabilize this form, while the C terminus of Bet3p invades the pocket to participate in its remodeling. The Trs31p subunit does not interact directly with the GTPase but allosterically regulates the TRAPPI interface with Ypt1p. Our findings imply that TRAPPII activates Ypt1p by an identical mechanism. This view of a multimeric membrane-tethering assembly complexed with a Rab provides a framework for understanding events preceding membrane fusion at the molecular level.
-===Crystal structure of a TRAPP subassembly activating the Rab Ypt1p===
+The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes.,Cai Y, Chin HF, Lazarova D, Menon S, Fu C, Cai H, Sclafani A, Rodgers DW, De La Cruz EM, Ferro-Novick S, Reinisch KM Cell. 2008 Jun 27;133(7):1202-13. PMID:18585354<ref>PMID:18585354</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3cue" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-CUE is a 24 chains 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=3CUE OCA].
+*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Cai, Y.]]
+[[Category: Cai Y]]
-[[Category: Reinisch, K M.]]
+[[Category: Reinisch KM]]
-[[Category: Acetylation]]
-[[Category: Cytoplasm]]
-[[Category: Endoplasmic reticulum]]
-[[Category: Er-golgi transport]]
-[[Category: Gef]]
-[[Category: Golgi apparatus]]
-[[Category: Gtp-binding]]
-[[Category: Guanine nucleotide exchange factor]]
-[[Category: Lipoprotein]]
-[[Category: Membrane traffic]]
-[[Category: Nucleotide-binding]]
-[[Category: Palmitate]]
-[[Category: Phosphoprotein]]
-[[Category: Prenylation]]
-[[Category: Protein transport]]
-[[Category: Rab activation]]
-[[Category: Tethering complex]]
-[[Category: Transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 03:43:27 2009''