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| | ==yeast Ent3_ENTH-Vti1p_Habc complex structure== | | ==yeast Ent3_ENTH-Vti1p_Habc complex structure== |
| - | <StructureSection load='3onl' size='340' side='right' caption='[[3onl]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='3onl' size='340' side='right'caption='[[3onl]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3onl]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ONL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ONL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3onl]] is a 3 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=3ONL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ONL FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3onj|3onj]], [[3onk|3onk]]</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]] 2.2Å</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=3onl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3onl OCA], [http://pdbe.org/3onl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3onl RCSB], [http://www.ebi.ac.uk/pdbsum/3onl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3onl 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=3onl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3onl OCA], [https://pdbe.org/3onl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3onl RCSB], [https://www.ebi.ac.uk/pdbsum/3onl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3onl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ENT3_YEAST ENT3_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> [[http://www.uniprot.org/uniprot/VTI1_YEAST VTI1_YEAST]] t-SNARE found in various SNARE complexes involved in multiple transport pathways. The composition of the t-SNARE complexes is specific for a limited number of v-SNAREs and therefore allows only the vesicles carrying the matching v-SNARE to fuse.<ref>PMID:10385523</ref> <ref>PMID:11739407</ref> <ref>PMID:14981247</ref> | + | [https://www.uniprot.org/uniprot/ENT3_YEAST ENT3_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 3onl" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3onl" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Epsin|Epsin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Fang, P]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Niu, L]] | + | [[Category: Fang P]] |
| - | [[Category: Teng, M]] | + | [[Category: Niu L]] |
| - | [[Category: Wang, J]] | + | [[Category: Teng M]] |
| - | [[Category: Enth]]
| + | [[Category: Wang J]] |
| - | [[Category: Habc]]
| + | |
| - | [[Category: Helix]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Recognition between snare and adaptor]]
| + | |
| Structural highlights
Function
ENT3_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
SNARE proteins are crucial for membrane fusion in vesicular transport. To ensure efficient and accurate fusion, SNAREs need to be sorted into different budding vesicles. This process is usually regulated by specific recognition between SNAREs and their adaptor proteins. How different pairs of SNAREs and adaptors achieve their recognition is unclear. Here, we report the recognition between yeast SNARE Vti1p and its adaptor Ent3p derived from three crystal structures. Surprisingly, this yeast pair Vti1p/Ent3p interacts through a distinct binding site compared to their homologues vti1b/epsinR in mammals. An opposite surface on Vti1p_Habc domain binds to a conserved area on the epsin N-terminal homology (ENTH) domain of Ent3p. Two-hybrid, in vitro pull-down and in vivo experiments indicate this binding interface is important for correct localization of Vti1p in the cell. This previously undescribed discovery that a cargo and adaptor pair uses different binding sites across species suggests the diversity of SNARE-adaptor recognition in vesicular transport.
Epsin N-terminal homology domains bind on opposite sides of two SNAREs.,Wang J, Gossing M, Fang P, Zimmermann J, Li X, von Mollard GF, Niu L, Teng M Proc Natl Acad Sci U S A. 2011 Jul 26;108(30):12277-82. Epub 2011 Jul 11. PMID:21746902[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
- ↑ Wang J, Gossing M, Fang P, Zimmermann J, Li X, von Mollard GF, Niu L, Teng M. Epsin N-terminal homology domains bind on opposite sides of two SNAREs. Proc Natl Acad Sci U S A. 2011 Jul 26;108(30):12277-82. Epub 2011 Jul 11. PMID:21746902 doi:10.1073/pnas.1013101108
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