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| | <StructureSection load='1w7p' size='340' side='right'caption='[[1w7p]], [[Resolution|resolution]] 3.60Å' scene=''> | | <StructureSection load='1w7p' size='340' side='right'caption='[[1w7p]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1w7p]] is a 4 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=1W7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W7P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1w7p]] 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=1W7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W7P FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1u5t|1u5t]]</div></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]] 3.6Å</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=1w7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7p OCA], [https://pdbe.org/1w7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w7p RCSB], [https://www.ebi.ac.uk/pdbsum/1w7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7p 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=1w7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7p OCA], [https://pdbe.org/1w7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w7p RCSB], [https://www.ebi.ac.uk/pdbsum/1w7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SNF8_YEAST SNF8_YEAST]] Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. [[https://www.uniprot.org/uniprot/VPS36_YEAST VPS36_YEAST]] Component of the ESCRT-II complex, which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Involved in the trafficking of the plasma membrane ATPase. Its ability to bind ubiquitin plays a central role in endosomal sorting of ubiquitinated cargo proteins by the ESCRT complexes.<ref>PMID:12194858</ref> [[https://www.uniprot.org/uniprot/VPS25_YEAST VPS25_YEAST]] Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex.<ref>PMID:12194858</ref>
| + | [https://www.uniprot.org/uniprot/SNF8_YEAST SNF8_YEAST] Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gonzalez, B]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Perisic, O]] | + | [[Category: Gonzalez B]] |
| - | [[Category: Teo, H]] | + | [[Category: Perisic O]] |
| - | [[Category: Williams, R L]] | + | [[Category: Teo H]] |
| - | [[Category: Endosomal protein sorting]]
| + | [[Category: Williams RL]] |
| - | [[Category: Escrt-ii complex]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| Structural highlights
Function
SNF8_YEAST Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex.
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
ESCRT-I, -II, and -III protein complexes are sequentially recruited to endosomal membranes, where they orchestrate protein sorting and MVB biogenesis. In addition, they play a critical role in retrovirus budding. Structural understanding of ESCRT interaction networks is largely lacking. The 3.6 A structure of the yeast ESCRT-II core presented here reveals a trilobal complex containing two copies of Vps25, one copy of Vps22, and the C-terminal region of Vps36. Unexpectedly, the entire ESCRT-II core consists of eight repeats of a common building block, a "winged helix" domain. Two PPXY-motifs from Vps25 are involved in contacts with Vps22 and Vps36, and their mutation leads to ESCRT-II disruption. We show that purified ESCRT-II binds directly to the Vps20 component of ESCRT-III. Surprisingly, this binding does not require the protruding N-terminal coiled-coil of Vps22. Vps25 is the chief subunit responsible for Vps20 recruitment. This interaction dramatically increases binding of both components to lipid vesicles in vitro.
ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes.,Teo H, Perisic O, Gonzalez B, Williams RL Dev Cell. 2004 Oct;7(4):559-69. PMID:15469844[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Teo H, Perisic O, Gonzalez B, Williams RL. ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes. Dev Cell. 2004 Oct;7(4):559-69. PMID:15469844 doi:10.1016/j.devcel.2004.09.003
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