3pr6

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Revision as of 13:33, 1 March 2024

Crystal structure analysis of yeast TRAPP associate protein Tca17

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Categories: Large Structures | Saccharomyces cerevisiae | Gohlke U | Heinemann U | Wang C

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 <StructureSection load='3pr6' size='340' side='right'caption='[[3pr6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3pr6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PR6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3pr6]] is a 1 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=3PR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PR6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SYGP-ORF36, TCA17, YEL048C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3pr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pr6 OCA], [https://pdbe.org/3pr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pr6 RCSB], [https://www.ebi.ac.uk/pdbsum/3pr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pr6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/TCA17_YEAST TCA17_YEAST]] Required, together with the TRAPP II subunit TRS33, for TRAPP II complex assembly or stability, and for proper Golgi localization of TRAPP and the Rab GTPase YPT31.<ref>PMID:19220810</ref> <ref>PMID:19416478</ref>
+[https://www.uniprot.org/uniprot/TCA17_YEAST TCA17_YEAST] Required, together with the TRAPP II subunit TRS33, for TRAPP II complex assembly or stability, and for proper Golgi localization of TRAPP and the Rab GTPase YPT31.<ref>PMID:19220810</ref> <ref>PMID:19416478</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The transport protein particle (TRAPP) is a hetero-multimeric complex involved in the trafficking of COP II (coat protein complex-II) vesicles. TRAPP is present in different eukaryotes from yeast to vertebrates and occurs in three distinct modifications with function in different intracellular transport steps. All forms contain a core of five essential subunits, and the different species of TRAPP are formed by the addition of various subunits. A recently identified TRAPP-associated protein, Tca17, is supposed to be involved in the regulation of the transport complex. We have determined the three-dimensional structure of yeast Tca17 by X-ray crystallography at a resolution of 1.8 A. It adopts the longin fold characteristic for the Bet5 family of TRAPP subunits, and it also shares a binding motif of these for the interaction with other members of the complex. Two alternative models of the localization of Tca17 within TRAPP as well as its potential role in the regulation of TRAPP function by transient integration into the complex are discussed. This article is protected by copyright. All rights reserved.
-Crystal structure of the yeast TRAPP-associated protein Tca17.,Wang C, Gohlke U, Roske Y, Heinemann U FEBS J. 2014 Jun 24. doi: 10.1111/febs.12888. PMID:24961828<ref>PMID:24961828</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3pr6" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Gohlke, U]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Heinemann, U]]
+[[Category: Gohlke U]]
-[[Category: Wang, C]]
+[[Category: Heinemann U]]
-[[Category: Longin fold]]
+[[Category: Wang C]]
-[[Category: Trans-golgi network]]
-[[Category: Transport protein]]
-[[Category: Trapp complex]]
-[[Category: Vesicle tethering regulation]]

3pr6

From Proteopedia

Revision as of 13:33, 1 March 2024

Crystal structure analysis of yeast TRAPP associate protein Tca17

Structural highlights

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