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5cw5

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==Structure of CfBRCC36-CfKIAA0157 complex (QSQ mutant)==
==Structure of CfBRCC36-CfKIAA0157 complex (QSQ mutant)==
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<StructureSection load='5cw5' size='340' side='right' caption='[[5cw5]], [[Resolution|resolution]] 2.74&Aring;' scene=''>
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<StructureSection load='5cw5' size='340' side='right'caption='[[5cw5]], [[Resolution|resolution]] 2.74&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5cw5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Camfo Camfo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CW5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CW5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5cw5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Camponotus_floridanus Camponotus floridanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CW5 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cw6|5cw6]], [[5cw4|5cw4]], [[5cw3|5cw3]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.736&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EAG_15736 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=104421 CAMFO]), EAG_01033 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=104421 CAMFO])</td></tr>
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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=5cw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cw5 OCA], [https://pdbe.org/5cw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cw5 RCSB], [https://www.ebi.ac.uk/pdbsum/5cw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cw5 ProSAT]</span></td></tr>
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<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=5cw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cw5 OCA], [http://pdbe.org/5cw5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cw5 RCSB], [http://www.ebi.ac.uk/pdbsum/5cw5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cw5 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/BRCC3_CAMFO BRCC3_CAMFO] Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates. Catalytic subunit of the BRISC complex; does not have activity by itself, but needs to be associated into a heterotetramer with ABRAXAS2 for minimal in vitro activity (PubMed:26344097). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating spindle assembly factors (By similarity).[UniProtKB:Q15018][UniProtKB:Q3TCJ1]<ref>PMID:26344097</ref>
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BRCC36 is a Zn(2+)-dependent deubiquitinating enzyme (DUB) that hydrolyzes lysine-63-linked ubiquitin chains as part of distinct macromolecular complexes that participate in either interferon signaling or DNA-damage recognition. The MPN(+) domain protein BRCC36 associates with pseudo DUB MPN(-) proteins KIAA0157 or Abraxas, which are essential for BRCC36 enzymatic activity. To understand the basis for BRCC36 regulation, we have solved the structure of an active BRCC36-KIAA0157 heterodimer and an inactive BRCC36 homodimer. Structural and functional characterizations show how BRCC36 is switched to an active conformation by contacts with KIAA0157. Higher-order association of BRCC36 and KIAA0157 into a dimer of heterodimers (super dimers) was required for DUB activity and interaction with targeting proteins SHMT2 and RAP80. These data provide an explanation of how an inactive pseudo DUB allosterically activates a cognate DUB partner and implicates super dimerization as a new regulatory mechanism underlying BRCC36 DUB activity, subcellular localization, and biological function.
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Higher-Order Assembly of BRCC36-KIAA0157 Is Required for DUB Activity and Biological Function.,Zeqiraj E, Tian L, Piggott CA, Pillon MC, Duffy NM, Ceccarelli DF, Keszei AF, Lorenzen K, Kurinov I, Orlicky S, Gish GD, Heck AJ, Guarne A, Greenberg RA, Sicheri F Mol Cell. 2015 Sep 17;59(6):970-83. doi: 10.1016/j.molcel.2015.07.028. Epub 2015 , Sep 3. PMID:26344097<ref>PMID:26344097</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 5cw5" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Camfo]]
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[[Category: Camponotus floridanus]]
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[[Category: Zeqiraj, E]]
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[[Category: Large Structures]]
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[[Category: Metal binding protein]]
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[[Category: Zeqiraj E]]
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[[Category: Metal dependent enzyme]]
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Current revision

Structure of CfBRCC36-CfKIAA0157 complex (QSQ mutant)

PDB ID 5cw5

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