2j9v
From Proteopedia
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<StructureSection load='2j9v' size='340' side='right'caption='[[2j9v]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2j9v' size='340' side='right'caption='[[2j9v]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2j9v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2j9v]] is a 1 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=2J9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J9V 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]] 2Å</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=2j9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j9v OCA], [https://pdbe.org/2j9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j9v RCSB], [https://www.ebi.ac.uk/pdbsum/2j9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j9v 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=2j9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j9v OCA], [https://pdbe.org/2j9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j9v RCSB], [https://www.ebi.ac.uk/pdbsum/2j9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j9v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/VPS28_YEAST VPS28_YEAST] Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for normal endocytic and biosynthetic traffic to the yeast vacuole. | ||
== 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=2j9v 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=2j9v ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | ESCRT (endosomal sorting complex required for transport) complexes orchestrate efficient sorting of ubiquitinated transmembrane receptors to lysosomes via multivesicular bodies (MVBs). Yeast ESCRT-I and ESCRT-II interact directly in vitro; however, this association is not detected in yeast cytosol. To gain understanding of the molecular mechanisms of this link, we have characterised the ESCRT-I/-II supercomplex and determined the crystal structure of its interface. The link is formed by the vacuolar protein sorting (Vps)28 C-terminus (ESCRT-I) binding with nanomolar affinity to the Vps36-NZF-N zinc-finger domain (ESCRT-II). A hydrophobic patch on the Vps28-CT four-helix bundle contacts the hydrophobic knuckles of Vps36-NZF-N. Mutation of the ESCRT-I/-II link results in a cargo-sorting defect in yeast. Interestingly, the two Vps36 NZF domains, NZF-N and NZF-C, despite having the same core fold, use distinct surfaces to bind ESCRT-I or ubiquitinated cargo. We also show that a new component of ESCRT-I, Mvb12 (YGR206W), engages ESCRT-I directly with nanomolar affinity to form a 1:1:1:1 heterotetramer. Mvb12 does not affect the affinity of ESCRT-I for ESCRT-II in vitro. Our data suggest a complex regulatory mechanism for the ESCRT-I/-II link in yeast. | ||
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| - | Structural insight into the ESCRT-I/-II link and its role in MVB trafficking.,Gill DJ, Teo H, Sun J, Perisic O, Veprintsev DB, Emr SD, Williams RL EMBO J. 2007 Jan 24;26(2):600-12. Epub 2007 Jan 11. PMID:17215868<ref>PMID:17215868</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2j9v" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]] | *[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Emr | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Gill | + | [[Category: Emr SD]] |
| - | [[Category: Perisic | + | [[Category: Gill DJ]] |
| - | [[Category: Sun | + | [[Category: Perisic O]] |
| - | [[Category: Teo | + | [[Category: Sun J]] |
| - | [[Category: Veprintsev | + | [[Category: Teo HL]] |
| - | [[Category: Williams | + | [[Category: Veprintsev DB]] |
| - | + | [[Category: Williams RL]] | |
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Current revision
2 Angstrom X-ray structure of the yeast ESCRT-I Vps28 C-terminus
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