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New page: left|200px<br /> <applet load="1w4u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w4u" /> '''NMR SOLUTION STRUCTURE OF THE UBIQUITIN CON...
 
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[[Image:1w4u.gif|left|200px]]<br />
<applet load="1w4u" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1w4u" />
'''NMR SOLUTION STRUCTURE OF THE UBIQUITIN CONJUGATING ENZYME UBCH5B'''<br />


==Overview==
==NMR solution structure of the ubiquitin conjugating enzyme UbcH5B==
The ubiquitination pathway is the main pathway for protein degradation in, eukaryotic cells. The attachment of ubiquitin to a substrate protein is, catalyzed by three types of enzymes, namely a ubiquitin activating enzyme, (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin ligase (E3)., Here, the structure of the human ubiquitin-conjugating enzyme (E2) UbcH5B, has been solved by a combination of homology modeling, NMR relaxation data, and automated NOE assignments. Comparison to E2 structures solved, previously by X-ray crystallography or NMR shows in all cases the same, compact fold, but differences are observed in the orientation of both N, and C-terminal alpha-helices. The N-terminal helix that is involved in, binding to ubiquitin ligases (E3) displays a different position, which, could have consequences for precise E2-E3 recognition. In addition, multiple conformations of the side-chain of Asn77 are found in solution, which contrasts the single hydrogen-bonded conformation in the crystal, structures of E2 enzymes. The possible implication of this conformational, freedom of Asn77 for its catalytic function is discussed.
<StructureSection load='1w4u' size='340' side='right'caption='[[1w4u]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1w4u]] 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=1W4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W4U 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=1w4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w4u OCA], [https://pdbe.org/1w4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w4u RCSB], [https://www.ebi.ac.uk/pdbsum/1w4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w4u ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UB2D2_HUMAN UB2D2_HUMAN] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3.<ref>PMID:10329681</ref> <ref>PMID:15280377</ref> <ref>PMID:18042044</ref> <ref>PMID:18703417</ref> <ref>PMID:18359941</ref> <ref>PMID:19854139</ref> <ref>PMID:20403326</ref> <ref>PMID:20061386</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/w4/1w4u_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=1w4u ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The ubiquitination pathway is the main pathway for protein degradation in eukaryotic cells. The attachment of ubiquitin to a substrate protein is catalyzed by three types of enzymes, namely a ubiquitin activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin ligase (E3). Here, the structure of the human ubiquitin-conjugating enzyme (E2) UbcH5B has been solved by a combination of homology modeling, NMR relaxation data and automated NOE assignments. Comparison to E2 structures solved previously by X-ray crystallography or NMR shows in all cases the same compact fold, but differences are observed in the orientation of both N and C-terminal alpha-helices. The N-terminal helix that is involved in binding to ubiquitin ligases (E3) displays a different position, which could have consequences for precise E2-E3 recognition. In addition, multiple conformations of the side-chain of Asn77 are found in solution, which contrasts the single hydrogen-bonded conformation in the crystal structures of E2 enzymes. The possible implication of this conformational freedom of Asn77 for its catalytic function is discussed.


==About this Structure==
Solution structure of the ubiquitin-conjugating enzyme UbcH5B.,Houben K, Dominguez C, van Schaik FM, Timmers HT, Bonvin AM, Boelens R J Mol Biol. 2004 Nov 19;344(2):513-26. PMID:15522302<ref>PMID:15522302</ref>
1W4U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W4U OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of the ubiquitin-conjugating enzyme UbcH5B., Houben K, Dominguez C, van Schaik FM, Timmers HT, Bonvin AM, Boelens R, J Mol Biol. 2004 Nov 19;344(2):513-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15522302 15522302]
</div>
<div class="pdbe-citations 1w4u" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ubiquitin--protein ligase]]
[[Category: Boelens R]]
[[Category: Boelens, R.]]
[[Category: Bonvin AMJJ]]
[[Category: Bonvin, A.M.J.J.]]
[[Category: Dominguez C]]
[[Category: Dominguez, C.]]
[[Category: Houben K]]
[[Category: Houben, K.]]
[[Category: Timmers HTM]]
[[Category: Schaik, F.M.A.Van.]]
[[Category: Van Schaik FMA]]
[[Category: Timmers, H.T.M.]]
[[Category: bl conjugation pathway]]
[[Category: e2 enzyme]]
[[Category: ligase]]
[[Category: ubiquitination]]
 
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