1yx4

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[[Image:1yx4.gif|left|200px]]
 
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{{Structure
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==Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition==
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|PDB= 1yx4 |SIZE=350|CAPTION= <scene name='initialview01'>1yx4</scene>
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<StructureSection load='1yx4' size='340' side='right'caption='[[1yx4]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= PSMD4, MCB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<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>
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}}
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yx/1yx4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1yx4" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Proteasome 3D structures|Proteasome 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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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]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Walters, K J.]]
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[[Category: Walters KJ]]
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[[Category: Wang, Q.]]
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[[Category: Wang Q]]
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[[Category: Young, P.]]
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[[Category: Young P]]
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[[Category: nmr]]
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[[Category: polyubiquitin]]
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[[Category: proteasome]]
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[[Category: s5a]]
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[[Category: uim]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:28:34 2008''
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Current revision

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

PDB ID 1yx4

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