2lbc: Difference between revisions
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<StructureSection load='2lbc' size='340' side='right' caption='[[2lbc]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | <StructureSection load='2lbc' size='340' side='right' caption='[[2lbc]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2lbc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LBC OCA]. <br> | <table><tr><td colspan='2'>[[2lbc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LBC FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">USP13, ISOT3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">USP13, ISOT3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lbc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lbc RCSB], [http://www.ebi.ac.uk/pdbsum/2lbc PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lbc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lbc RCSB], [http://www.ebi.ac.uk/pdbsum/2lbc PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin.,Zhang YH, Zhou CJ, Zhou ZR, Song AX, Hu HY PLoS One. 2011;6(12):e29362. Epub 2011 Dec 28. PMID:22216260<ref>PMID:22216260</ref> | Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin.,Zhang YH, Zhou CJ, Zhou ZR, Song AX, Hu HY PLoS One. 2011;6(12):e29362. Epub 2011 Dec 28. PMID:22216260<ref>PMID:22216260</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
==See Also== | |||
*[[Thioesterase|Thioesterase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Ubiquitinyl hydrolase 1]] | [[Category: Ubiquitinyl hydrolase 1]] | ||
[[Category: Hu, H | [[Category: Hu, H]] | ||
[[Category: Song, A | [[Category: Song, A]] | ||
[[Category: Zhang, Y | [[Category: Zhang, Y]] | ||
[[Category: Zhou, C | [[Category: Zhou, C]] | ||
[[Category: Zhou, Z | [[Category: Zhou, Z]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Tandem uba of usp13]] | [[Category: Tandem uba of usp13]] | ||
Revision as of 09:26, 22 December 2014
solution structure of tandem UBA of USP13solution structure of tandem UBA of USP13
Structural highlights
Publication Abstract from PubMedDeubiquitination is a reverse process of cellular ubiquitination important for many biological events. Ubiquitin (Ub)-specific protease 13 (USP13) is an ortholog of USP5 implicated in catalyzing hydrolysis of various Ub chains, but its enzymatic properties and catalytic regulation remain to be explored. Here we report studies of the roles of the Ub-binding domains of USP13 in regulatory catalysis by biochemical and NMR structural approaches. Our data demonstrate that USP13, distinct from USP5, exhibits a weak deubiquitinating activity preferring to Lys63-linked polyubiquitin (K63-polyUb) in a non-activation manner. The zinc finger (ZnF) domain of USP13 shares a similar fold with that of USP5, but it cannot bind with Ub, so that USP13 has lost its ability to be activated by free Ub. Substitution of the ZnF domain with that of USP5 confers USP13 the property of catalytic activation. The tandem Ub-associated (UBA) domains of USP13 can bind with different types of diUb but preferentially with K63-linked, providing a possible explanation for the weak activity preferring to K63-polyUb. USP13 can also regulate the protein level of CD3delta in cells, probably depending on its weak deubiquitinating activity and the Ub-binding properties of the UBA domains. Thus, the non-activating catalysis of USP13 for K63-polyUb chains implies that it may function differently from USP5 in cellular deubiquitination processes. Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin.,Zhang YH, Zhou CJ, Zhou ZR, Song AX, Hu HY PLoS One. 2011;6(12):e29362. Epub 2011 Dec 28. PMID:22216260[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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