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New page: left|200px<br /><applet load="2f66" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f66, resolution 2.80Å" /> '''Structure of the ESC...
 
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[[Image:2f66.gif|left|200px]]<br /><applet load="2f66" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2f66, resolution 2.80&Aring;" />
'''Structure of the ESCRT-I endosomal trafficking complex'''<br />


==Overview==
==Structure of the ESCRT-I endosomal trafficking complex==
The 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.
<StructureSection load='2f66' size='340' side='right'caption='[[2f66]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2f66]] is a 6 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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='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>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/2f66_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2f66 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 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.


==About this Structure==
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<ref>PMID:16615894</ref>
2F66 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F66 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16615894 16615894]
</div>
[[Category: Protein complex]]
<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/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Hurley, J.H.]]
[[Category: Hurley JH]]
[[Category: Kim, J.]]
[[Category: Kim J]]
[[Category: Kostelansky, M.S.]]
[[Category: Kostelansky MS]]
[[Category: Lee, S.]]
[[Category: Lee S]]
[[Category: SO4]]
[[Category: endosomal sorting complex required for transport]]
[[Category: endosome]]
[[Category: escrt protein complexes]]
[[Category: escrt-i]]
[[Category: trafficking complex]]
[[Category: tsg101]]
[[Category: ubiquitin]]
[[Category: vacuolar protein sorting]]
[[Category: vps23]]
[[Category: vps28]]
[[Category: vps37]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:23:10 2007''

Latest revision as of 07:43, 23 August 2023

Structure of the ESCRT-I endosomal trafficking complex

2f66, resolution 2.80Å

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