2f66: Difference between revisions
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==Structure of the ESCRT-I endosomal trafficking complex== | ==Structure of the ESCRT-I endosomal trafficking complex== | ||
<StructureSection load='2f66' size='340' side='right' caption='[[2f66]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='2f66' size='340' side='right'caption='[[2f66]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2f66]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2f66]] is a 6 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=2F66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F66 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u5t|1u5t]], [[1uzx|1uzx]], [[1w7p|1w7p]], [[1xb4|1xb4]]</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]], [[1uzx|1uzx]], [[1w7p|1w7p]], [[1xb4|1xb4]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STP22, VPS23 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STP22, VPS23 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), VPS28, VPT28 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), SRN2, VPS37 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f66 OCA], [https://pdbe.org/2f66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f66 RCSB], [https://www.ebi.ac.uk/pdbsum/2f66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f66 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/STP22_YEAST STP22_YEAST]] Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association to the ESCRT-0 complex. Required for vacuolar targeting of temperature-sensitive plasma membrane proteins STE2 and CAN1.<ref>PMID:10207082</ref> <ref>PMID:11208108</ref> <ref>PMID:11511343</ref> [[https://www.uniprot.org/uniprot/SRN2_YEAST SRN2_YEAST]] Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for normal endocytic and biosynthetic traffic to the yeast vacuole. [[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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</div> | </div> | ||
<div class="pdbe-citations 2f66" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2f66" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 18824]] | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | |||
[[Category: Hurley, J H]] | [[Category: Hurley, J H]] | ||
[[Category: Kim, J]] | [[Category: Kim, J]] | ||
Revision as of 13:38, 17 February 2021
Structure of the ESCRT-I endosomal trafficking complexStructure of the ESCRT-I endosomal trafficking complex
Structural highlights
Function[STP22_YEAST] Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association to the ESCRT-0 complex. Required for vacuolar targeting of temperature-sensitive plasma membrane proteins STE2 and CAN1.[1] [2] [3] [SRN2_YEAST] Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for normal endocytic and biosynthetic traffic to the yeast vacuole. [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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe endosomal sorting complex required for transport (ESCRT) complexes are central to receptor downregulation, lysosome biogenesis, and budding of HIV. The yeast ESCRT-I complex contains the Vps23, Vps28, and Vps37 proteins, and its assembly is directed by the C-terminal steadiness box of Vps23, the N-terminal half of Vps28, and the C-terminal half of Vps37. The crystal structures of a Vps23:Vps28 core subcomplex and the Vps23:Vps28:Vps37 core were solved at 2.1 and 2.8 A resolution. Each subunit contains a structurally similar pair of helices that form the core. The N-terminal domain of Vps28 has a hydrophobic binding site on its surface that is conformationally dynamic. The C-terminal domain of Vps28 binds the ESCRT-II complex. The structure shows how ESCRT-I is assembled by a compact core from which the Vps23 UEV domain, the Vps28 C domain, and other domains project to bind their partners. Structural and functional organization of the ESCRT-I trafficking complex.,Kostelansky MS, Sun J, Lee S, Kim J, Ghirlando R, Hierro A, Emr SD, Hurley JH Cell. 2006 Apr 7;125(1):113-26. PMID:16615894[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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