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| | <StructureSection load='5cmy' size='340' side='right'caption='[[5cmy]], [[Resolution|resolution]] 2.09Å' scene=''> | | <StructureSection load='5cmy' size='340' side='right'caption='[[5cmy]], [[Resolution|resolution]] 2.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cmy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CMY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CMY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cmy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CMY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.09Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cmw|5cmw]]</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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ENT5, YDR153C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=5cmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmy OCA], [https://pdbe.org/5cmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cmy RCSB], [https://www.ebi.ac.uk/pdbsum/5cmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cmy ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmy OCA], [http://pdbe.org/5cmy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cmy RCSB], [http://www.ebi.ac.uk/pdbsum/5cmy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cmy ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ENT5_YEAST ENT5_YEAST]] Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB).<ref>PMID:12483220</ref> <ref>PMID:15107463</ref> | + | [https://www.uniprot.org/uniprot/ENT5_YEAST ENT5_YEAST] Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB).<ref>PMID:12483220</ref> <ref>PMID:15107463</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5cmy" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5cmy" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Epsin|Epsin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Li, X]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Song, Y]] | + | [[Category: Li X]] |
| - | [[Category: Teng, M K]] | + | [[Category: Song Y]] |
| - | [[Category: Zhang, F]] | + | [[Category: Teng MK]] |
| - | [[Category: Ent5]]
| + | [[Category: Zhang F]] |
| - | [[Category: Inositol phosphate]]
| + | |
| - | [[Category: N-terminal domain]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Vesicular transport]]
| + | |
| Structural highlights
Function
ENT5_YEAST Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB).[1] [2]
Publication Abstract from PubMed
Clathrin-coated vesicles (CCVs) play critical roles in multiple cellular processes, including nutrient uptake, endosome/lysosome biogenesis, pathogen invasion, regulation of signalling receptors, etc. Saccharomyces cerevisiae Ent5 (ScEnt5) is one of the two major adaptors supporting the CCV-mediated TGN/endosome traffic in yeast cells. However, the classification and phosphoinositide binding characteristic of ScEnt5 remain elusive. Here we report the crystal structures of the ScEnt5 N-terminal domain, and find that ScEnt5 contains an insertion alpha' helix that does not exist in other ENTH or ANTH domains. Furthermore, we investigate the classification of ScEnt5-N(31-191) by evolutionary history analyses and structure comparisons, and find that the ScEnt5 N-terminal domain shows different phosphoinositide binding property from rEpsin1 and rCALM. Above results facilitate the understanding of the ScEnt5-mediated vesicle coat formation process.
Structural and functional insight into the N-terminal domain of the clathrin adaptor Ent5 from Saccharomyces cerevisiae.,Zhang F, Song Y, Ebrahimi M, Niu L, Teng M, Li X Biochem Biophys Res Commun. 2016 Sep 2;477(4):786-93. doi:, 10.1016/j.bbrc.2016.06.136. Epub 2016 Jun 28. PMID:27369074[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Duncan MC, Costaguta G, Payne GS. Yeast epsin-related proteins required for Golgi-endosome traffic define a gamma-adaptin ear-binding motif. Nat Cell Biol. 2003 Jan;5(1):77-81. PMID:12483220 doi:http://dx.doi.org/10.1038/ncb901
- ↑ Eugster A, Pecheur EI, Michel F, Winsor B, Letourneur F, Friant S. Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. Mol Biol Cell. 2004 Jul;15(7):3031-41. Epub 2004 Apr 23. PMID:15107463 doi:10.1091/mbc.E03-11-0793
- ↑ Zhang F, Song Y, Ebrahimi M, Niu L, Teng M, Li X. Structural and functional insight into the N-terminal domain of the clathrin adaptor Ent5 from Saccharomyces cerevisiae. Biochem Biophys Res Commun. 2016 Sep 2;477(4):786-93. doi:, 10.1016/j.bbrc.2016.06.136. Epub 2016 Jun 28. PMID:27369074 doi:http://dx.doi.org/10.1016/j.bbrc.2016.06.136
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