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| <StructureSection load='1u5t' size='340' side='right'caption='[[1u5t]], [[Resolution|resolution]] 3.60Å' scene=''> | | <StructureSection load='1u5t' size='340' side='right'caption='[[1u5t]], [[Resolution|resolution]] 3.60Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1u5t]] 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=1U5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U5T FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1u5t]] 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=1U5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U5T FirstGlance]. <br> |
| </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=1u5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u5t OCA], [https://pdbe.org/1u5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u5t RCSB], [https://www.ebi.ac.uk/pdbsum/1u5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u5t ProSAT]</span></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=1u5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u5t OCA], [https://pdbe.org/1u5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u5t RCSB], [https://www.ebi.ac.uk/pdbsum/1u5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u5t 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/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/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/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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| </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=1u5t 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=1u5t ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The multivesicular-body (MVB) pathway delivers transmembrane proteins and lipids to the lumen of the endosome. The multivesicular-body sorting pathway has crucial roles in growth-factor-receptor downregulation, developmental signalling, regulation of the immune response and the budding of certain enveloped viruses such as human immunodeficiency virus. Ubiquitination is a signal for sorting into the MVB pathway, which also requires the functions of three protein complexes, termed ESCRT-I, -II and -III (endosomal sorting complex required for transport). Here we report the crystal structure of the core of the yeast ESCRT-II complex, which contains one molecule of the Vps protein Vps22, the carboxy-terminal domain of Vps36 and two molecules of Vps25, and has the shape of a capital letter 'Y'. The amino-terminal coiled coil of Vps22 and the flexible linker leading to the ubiquitin-binding NZF domain of Vps36 both protrude from the tip of one branch of the 'Y'. Vps22 and Vps36 form nearly equivalent interactions with the two Vps25 molecules at the centre of the 'Y'. The structure suggests how ubiquitinated cargo could be passed between ESCRT components of the MVB pathway through the sequential transfer of ubiquitinated cargo from one complex to the next.
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| Structure of the ESCRT-II endosomal trafficking complex.,Hierro A, Sun J, Rusnak AS, Kim J, Prag G, Emr SD, Hurley JH Nature. 2004 Sep 9;431(7005):221-5. Epub 2004 Aug 25. PMID:15329733<ref>PMID:15329733</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1u5t" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 18824]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Emr, S D]] | | [[Category: Saccharomyces cerevisiae]] |
| [[Category: Hierro, A]] | | [[Category: Emr SD]] |
| [[Category: Hurley, J H]] | | [[Category: Hierro A]] |
| [[Category: Kim, J]] | | [[Category: Hurley JH]] |
| [[Category: Prag, G]] | | [[Category: Kim J]] |
| [[Category: Rusnak, A S]] | | [[Category: Prag G]] |
| [[Category: Sun, J]] | | [[Category: Rusnak AS]] |
| [[Category: Endosomal]]
| | [[Category: Sun J]] |
| [[Category: Escrt]]
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| [[Category: Protein complex]]
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| [[Category: Trafficking]]
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| [[Category: Transport protein]]
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