4w4u: Difference between revisions
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The | ==Structure of yeast SAGA DUBm with Sgf73 Y57A mutant at 2.8 angstroms resolution== | ||
<StructureSection load='4w4u' size='340' side='right'caption='[[4w4u]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4w4u]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_CEN.PK113-7D Saccharomyces cerevisiae CEN.PK113-7D] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W4U FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4w4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w4u OCA], [https://pdbe.org/4w4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w4u RCSB], [https://www.ebi.ac.uk/pdbsum/4w4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w4u ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/N1P0J5_YEASC N1P0J5_YEASC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The SAGA (Spt-Ada-Gcn5 acetyltransferase) complex performs multiple functions in transcription activation including deubiquitinating histone H2B, which is mediated by a subcomplex called the deubiquitinating module (DUBm). The yeast DUBm comprises a catalytic subunit, Ubp8, and three additional subunits, Sgf11, Sus1 and Sgf73, all of which are required for DUBm activity. A portion of the non-globular Sgf73 subunit lies between the Ubp8 catalytic domain and the ZnF-UBP domain and has been proposed to contribute to deubiquitinating activity by maintaining the catalytic domain in an active conformation. We report structural and solution studies of the DUBm containing two different Sgf73 point mutations that disrupt deubiquitinating activity. We find that the Sgf73 mutations abrogate deubiquitinating activity by impacting the Ubp8 ubiquitin-binding fingers region and they have an unexpected effect on the overall folding and stability of the DUBm complex. Taken together, our data suggest a role for Sgf73 in maintaining both the organization and the ubiquitin-binding conformation of Ubp8, thereby contributing to overall DUBm activity. | |||
Uncovering the role of Sgf73 in maintaining SAGA deubiquitinating module structure and activity.,Yan M, Wolberger C J Mol Biol. 2015 Apr 24;427(8):1765-78. doi: 10.1016/j.jmb.2014.12.004. Epub 2014, Dec 17. PMID:25526805<ref>PMID:25526805</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4w4u" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[SAGA-associated factor|SAGA-associated factor]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae CEN PK113-7D]] | |||
[[Category: Saccharomyces cerevisiae S288C]] | |||
[[Category: Wolberger C]] | |||
[[Category: Yan M]] | |||