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4p0p
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(Difference between revisions)
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| - | ''' | + | ==Crystal structure of Human Mus81-Eme1 in complex with 5'-flap DNA, and Mg2+== |
| + | <StructureSection load='4p0p' size='340' side='right' caption='[[4p0p]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4p0p]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P0P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P0P FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p0q|4p0q]], [[4p0r|4p0r]], [[4p0s|4p0s]]</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=4p0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p0p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p0p RCSB], [http://www.ebi.ac.uk/pdbsum/4p0p PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Mus81-Eme1 complex is a structure-selective endonuclease with a critical role in the resolution of recombination intermediates during DNA repair after interstrand cross-links, replication fork collapse, or double-strand breaks. To explain the molecular basis of 3' flap substrate recognition and cleavage mechanism by Mus81-Eme1, we determined crystal structures of human Mus81-Eme1 bound to various flap DNA substrates. Mus81-Eme1 undergoes gross substrate-induced conformational changes that reveal two key features: (i) a hydrophobic wedge of Mus81 that separates pre- and post-nick duplex DNA and (ii) a "5' end binding pocket" that hosts the 5' nicked end of post-nick DNA. These features are crucial for comprehensive protein-DNA interaction, sharp bending of the 3' flap DNA substrate, and incision strand placement at the active site. While Mus81-Eme1 unexpectedly shares several common features with members of the 5' flap nuclease family, the combined structural, biochemical, and biophysical analyses explain why Mus81-Eme1 preferentially cleaves 3' flap DNA substrates with 5' nicked ends. | ||
| - | + | Crystal structures of the structure-selective nuclease Mus81-Eme1 bound to flap DNA substrates.,Gwon GH, Jo A, Baek K, Jin KS, Fu Y, Lee JB, Kim Y, Cho Y EMBO J. 2014 May 2;33(9):1061-72. doi: 10.1002/embj.201487820. Epub 2014 Apr 14. PMID:24733841<ref>PMID:24733841</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Baek, K.]] | ||
| + | [[Category: Cho, Y.]] | ||
| + | [[Category: Gwon, G H.]] | ||
| + | [[Category: Hydroase-dna complex]] | ||
| + | [[Category: Hydrolase-dna complex]] | ||
| + | [[Category: Resolvase]] | ||
Revision as of 09:37, 28 May 2014
Crystal structure of Human Mus81-Eme1 in complex with 5'-flap DNA, and Mg2+
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