2zih
From Proteopedia
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<StructureSection load='2zih' size='340' side='right'caption='[[2zih]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='2zih' size='340' side='right'caption='[[2zih]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2zih]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2zih]] 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=2ZIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZIH FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zih OCA], [https://pdbe.org/2zih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zih RCSB], [https://www.ebi.ac.uk/pdbsum/2zih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zih 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=2zih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zih OCA], [https://pdbe.org/2zih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zih RCSB], [https://www.ebi.ac.uk/pdbsum/2zih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zih ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/VPS74_YEAST VPS74_YEAST] Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Mediates the cis and medial Golgi localization of mannosyltransferases through direct binding of their cytosolic domains. Involved in vacuolar protein sorting.<ref>PMID:20026658</ref> <ref>PMID:22889169</ref> <ref>PMID:18410729</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=2zih ConSurf]. | </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=2zih ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The mechanism of glycosyltransferase localization to the Golgi apparatus is a long-standing question in secretory cell biology. All Golgi glycosyltransferases are type II membrane proteins with small cytosolic domains that contribute to Golgi localization. To date, no protein has been identified that recognizes the cytosolic domains of Golgi enzymes and contributes to their localization. Here, we report that yeast Vps74p directly binds to the cytosolic domains of cis and medial Golgi mannosyltransferases and that loss of this interaction correlates with loss of Golgi localization of these enzymes. We have solved the X-ray crystal structure of Vps74p and find that it forms a tetramer, which we also observe in solution. Deletion of a critical structural motif disrupts tetramer formation and results in loss of Vps74p localization and function. Vps74p is highly homologous to the human GMx33 Golgi matrix proteins, suggesting a conserved function for these proteins in the Golgi enzyme localization machinery. | ||
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| - | Golgi localization of glycosyltransferases requires a Vps74p oligomer.,Schmitz KR, Liu J, Li S, Setty TG, Wood CS, Burd CG, Ferguson KM Dev Cell. 2008 Apr;14(4):523-34. PMID:18410729<ref>PMID:18410729</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2zih" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: | + | [[Category: Ferguson KM]] |
| - | [[Category: | + | [[Category: Li S]] |
| - | [[Category: | + | [[Category: Schmitz KR]] |
| - | [[Category: | + | [[Category: Setty TG]] |
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Current revision
Crystal Structure of Yeast Vps74
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