1yx4: Difference between revisions

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[[Image:1yx4.gif|left|200px]]


{{Structure
==Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition==
|PDB= 1yx4 |SIZE=350|CAPTION= <scene name='initialview01'>1yx4</scene>
<StructureSection load='1yx4' size='340' side='right'caption='[[1yx4]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1yx4]] is a 1 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=1YX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YX4 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE= PSMD4, MCB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yx4 OCA], [https://pdbe.org/1yx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yx4 RCSB], [https://www.ebi.ac.uk/pdbsum/1yx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yx4 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/1yx4_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=1yx4 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.


'''Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition'''
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1yx4" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Proteasome 3D structures|Proteasome 3D structures]]
 
== References ==
==About this Structure==
<references/>
1YX4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YX4 OCA].
__TOC__
 
</StructureSection>
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/15826667 15826667]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[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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