View source for 2mc3


==NMR solution structure of the winged-helix domain from MUS81 structure-specific endonuclease==
<StructureSection load='2mc3' size='340' side='right'caption='[[2mc3]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mc3]] 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=2MC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MC3 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=2mc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mc3 OCA], [https://pdbe.org/2mc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mc3 RCSB], [https://www.ebi.ac.uk/pdbsum/2mc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mc3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MUS81_HUMAN MUS81_HUMAN] Interacts with EME1 and EME2 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks.<ref>PMID:11741546</ref> <ref>PMID:12374758</ref> <ref>PMID:12686547</ref> <ref>PMID:12721304</ref> <ref>PMID:14617801</ref> <ref>PMID:15805243</ref> <ref>PMID:17289582</ref> <ref>PMID:19595721</ref> <ref>PMID:19596235</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The MUS81-EME1 endonuclease maintains metazoan genomic integrity by cleaving branched DNA structures that arise during the resolution of recombination intermediates. In humans, MUS81 also forms a poorly characterized complex with EME2. Here, we identify and determine the structure of a winged helix (WH) domain from human MUS81, which binds DNA. WH domain mutations greatly reduce binding of the isolated domain to DNA and impact on incision activity of MUS81-EME1/EME2 complexes. Deletion of the WH domain reduces the endonuclease activity of both MUS81-EME1 and MUS81-EME2 complexes, and incisions made by MUS81-EME2 are made closer to the junction on substrates containing a downstream duplex, such as fork structures and nicked Holliday junctions. WH domain mutation or deletion in Schizosaccharomyces pombe phenocopies the DNA-damage sensitivity of strains deleted for mus81. Our results indicate an important role for the WH domain in both yeast and human MUS81 complexes.

A winged helix domain in human MUS81 binds DNA and modulates the endonuclease activity of MUS81 complexes.,Fadden AJ, Schalbetter S, Bowles M, Harris R, Lally J, Carr AM, McDonald NQ Nucleic Acids Res. 2013 Aug 27. PMID:23982516<ref>PMID:23982516</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mc3" style="background-color:#fffaf0;"></div>

==See Also==
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Fadden A]]
[[Category: Harris R]]
[[Category: Mcdonald NQ]]