2p22: Difference between revisions

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[[Image:2p22.jpg|left|200px]]


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==Structure of the Yeast ESCRT-I Heterotetramer Core==
The line below this paragraph, containing "STRUCTURE_2p22", creates the "Structure Box" on the page.
<StructureSection load='2p22' size='340' side='right'caption='[[2p22]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2p22]] 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=2P22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P22 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<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>
{{STRUCTURE_2p22| PDB=2p22 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p22 OCA], [https://pdbe.org/2p22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p22 RCSB], [https://www.ebi.ac.uk/pdbsum/2p22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p22 ProSAT]</span></td></tr>
</table>
== 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>
== 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/p2/2p22_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=2p22 ConSurf].
<div style="clear:both"></div>


'''Structure of the Yeast ESCRT-I Heterotetramer Core'''
==See Also==
 
*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
 
== References ==
==Overview==
<references/>
The endosomal sorting complex required for transport-I (ESCRT-I) complex, which is conserved from yeast to humans, directs the lysosomal degradation of ubiquitinated transmembrane proteins and the budding of the HIV virus. Yeast ESCRT-I contains four subunits, Vps23, Vps28, Vps37, and Mvb12. The crystal structure of the heterotetrameric ESCRT-I complex reveals a highly asymmetric complex of 1:1:1:1 subunit stoichiometry. The core complex is nearly 18 nm long and consists of a headpiece attached to a 13 nm stalk. The stalk is important for cargo sorting by ESCRT-I and is proposed to serve as a spacer regulating the correct disposition of cargo and other ESCRT components. Hydrodynamic constraints and crystallographic structures were used to generate a model of intact ESCRT-I in solution. The results show how ESCRT-I uses a combination of a rigid stalk and flexible tethers to interact with lipids, cargo, and other ESCRT complexes over a span of approximately 25 nm.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2P22 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P22 OCA].
 
==Reference==
Molecular architecture and functional model of the complete yeast ESCRT-I heterotetramer., Kostelansky MS, Schluter C, Tam YY, Lee S, Ghirlando R, Beach B, Conibear E, Hurley JH, Cell. 2007 May 4;129(3):485-98. Epub 2007 Apr 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17442384 17442384]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Hurley, J H.]]
[[Category: Hurley JH]]
[[Category: Kostelansky, MS]]
[[Category: Kostelansky MS]]
[[Category: Endosomal sorting complex required for transport]]
[[Category: Endosome]]
[[Category: Escrt protein complex]]
[[Category: Escrt-i]]
[[Category: Mvb12]]
[[Category: Trafficking complex]]
[[Category: Tsg101]]
[[Category: Ubiquitin]]
[[Category: Vacuolar protein sorting]]
[[Category: Vps23]]
[[Category: Vps28]]
[[Category: Vps37]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 12:10:32 2008''
Retrieved from "https://proteopedia.org/2p22"