1yx5: Difference between revisions

New page: left|200px<br /> <applet load="1yx5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yx5" /> '''Solution Structure of S5a UIM-1/Ubiquitin C...
 
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[[Image:1yx5.gif|left|200px]]<br />
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'''Solution Structure of S5a UIM-1/Ubiquitin Complex'''<br />


==Overview==
==Solution Structure of S5a UIM-1/Ubiquitin Complex==
Ubiquitin is a key regulatory molecule in diverse cellular events. How, cells determine the outcome of ubiquitylation remains unclear; however, a, likely determinant is the specificity of ubiquitin receptor proteins for, polyubiquitin chains of certain length and linkage. Proteasome subunit S5a, contains two ubiquitin-interacting motifs (UIMs) through which it recruits, ubiquitylated substrates to the proteasome for their degradation. Here, we, report the structure of S5a (196-306) alone and complexed with two, monoubiquitin molecules. This construct contains the two UIMs of S5a and, we reveal their different ubiquitin-binding mechanisms and provide a, rationale for their unique specificities for different ubiquitin-like, domains. Furthermore, we provide direct evidence that S5a (196-306) binds, either K63-linked or K48-linked polyubiquitin, and in both cases prefers, longer chains. On the basis of these results we present a model for how, S5a and other ubiquitin-binding proteins recognize polyubiquitin.
<StructureSection load='1yx5' size='340' side='right'caption='[[1yx5]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1yx5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YX5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1yx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yx5 OCA], [https://pdbe.org/1yx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yx5 RCSB], [https://www.ebi.ac.uk/pdbsum/1yx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yx5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PSMD4_HUMAN PSMD4_HUMAN] Binds and presumably selects ubiquitin-conjugates for destruction. Displays selectivity for longer polyubiquitin chains. Modulates intestinal fluid secretion.
== 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/yx/1yx5_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=1yx5 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ubiquitin is a key regulatory molecule in diverse cellular events. How cells determine the outcome of ubiquitylation remains unclear; however, a likely determinant is the specificity of ubiquitin receptor proteins for polyubiquitin chains of certain length and linkage. Proteasome subunit S5a contains two ubiquitin-interacting motifs (UIMs) through which it recruits ubiquitylated substrates to the proteasome for their degradation. Here, we report the structure of S5a (196-306) alone and complexed with two monoubiquitin molecules. This construct contains the two UIMs of S5a and we reveal their different ubiquitin-binding mechanisms and provide a rationale for their unique specificities for different ubiquitin-like domains. Furthermore, we provide direct evidence that S5a (196-306) binds either K63-linked or K48-linked polyubiquitin, and in both cases prefers longer chains. On the basis of these results we present a model for how S5a and other ubiquitin-binding proteins recognize polyubiquitin.


==About this Structure==
Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition.,Wang Q, Young P, Walters KJ J Mol Biol. 2005 May 6;348(3):727-39. PMID:15826667<ref>PMID:15826667</ref>
1YX5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YX5 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition., Wang Q, Young P, Walters KJ, J Mol Biol. 2005 May 6;348(3):727-39. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15826667 15826667]
</div>
<div class="pdbe-citations 1yx5" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Proteasome 3D structures|Proteasome 3D structures]]
*[[3D structures of ubiquitin|3D structures of ubiquitin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Walters, K.J.]]
[[Category: Walters KJ]]
[[Category: Wang, Q.]]
[[Category: Wang Q]]
[[Category: Young, P.]]
[[Category: Young P]]
[[Category: nmr]]
[[Category: polyubiquitin]]
[[Category: proteasome]]
[[Category: s5a]]
[[Category: uim]]
 
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