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| | <StructureSection load='1wc9' size='340' side='right'caption='[[1wc9]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='1wc9' size='340' side='right'caption='[[1wc9]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1wc9]] is a 1 chain structure with sequence from [http://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=1WC9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1WC9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1wc9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WC9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</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]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wc8|1wc8]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1wc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wc9 OCA], [http://pdbe.org/1wc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wc9 RCSB], [http://www.ebi.ac.uk/pdbsum/1wc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wc9 ProSAT]</span></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=1wc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wc9 OCA], [https://pdbe.org/1wc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wc9 RCSB], [https://www.ebi.ac.uk/pdbsum/1wc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wc9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TPPC3_MOUSE TPPC3_MOUSE]] May play a role in vesicular transport from endoplasmic reticulum to Golgi. | + | [https://www.uniprot.org/uniprot/TPPC3_MOUSE TPPC3_MOUSE] May play a role in vesicular transport from endoplasmic reticulum to Golgi. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Kim, Y G]] | + | [[Category: Kim Y-G]] |
| - | [[Category: Lee, H S]] | + | [[Category: Lee H-S]] |
| - | [[Category: Oh, B H]] | + | [[Category: Oh B-H]] |
| - | [[Category: Sacher, M]] | + | [[Category: Sacher M]] |
| - | [[Category: Endoplasmic reticulum]]
| + | |
| - | [[Category: Golgi stack]]
| + | |
| - | [[Category: Tethering factor]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Trapp]]
| + | |
| - | [[Category: Vesicle transport]]
| + | |
| Structural highlights
Function
TPPC3_MOUSE May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Transport protein particle (TRAPP) is a large multiprotein complex involved in endoplasmic reticulum-to-Golgi and intra-Golgi traffic. TRAPP specifically and persistently resides on Golgi membranes. Neither the mechanism of the subcellular localization nor the function of any of the individual TRAPP components is known. Here, the crystal structure of mouse Bet3p (bet3), a conserved TRAPP component, reveals a dimeric structure with hydrophobic channels. The channel entrances are located on a putative membrane-interacting surface that is distinctively flat, wide and decorated with positively charged residues. Charge-inversion mutations on the flat surface of the highly conserved yeast Bet3p led to conditional lethality, incorrect localization and membrane trafficking defects. A channel-blocking mutation led to similar defects. These data delineate a molecular mechanism of Golgi-specific targeting and anchoring of Bet3p involving the charged surface and insertion of a Golgi-specific hydrophobic moiety into the channels. This essential subunit could then direct other TRAPP components to the Golgi.
Crystal structure of bet3 reveals a novel mechanism for Golgi localization of tethering factor TRAPP.,Kim YG, Sohn EJ, Seo J, Lee KJ, Lee HS, Hwang I, Whiteway M, Sacher M, Oh BH Nat Struct Mol Biol. 2005 Jan;12(1):38-45. Epub 2004 Dec 19. PMID:15608655[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim YG, Sohn EJ, Seo J, Lee KJ, Lee HS, Hwang I, Whiteway M, Sacher M, Oh BH. Crystal structure of bet3 reveals a novel mechanism for Golgi localization of tethering factor TRAPP. Nat Struct Mol Biol. 2005 Jan;12(1):38-45. Epub 2004 Dec 19. PMID:15608655 doi:10.1038/nsmb871
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