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4p0s

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4p0s]] is a 20 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P0S FirstGlance]. <br>
<table><tr><td colspan='2'>[[4p0s]] is a 20 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P0S FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p0p|4p0p]], [[4p0q|4p0q]], [[4p0r|4p0r]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p0p|4p0p]], [[4p0q|4p0q]], [[4p0r|4p0r]]</td></tr>
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<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=4p0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p0s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p0s RCSB], [http://www.ebi.ac.uk/pdbsum/4p0s PDBsum]</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=4p0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p0s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p0s RCSB], [http://www.ebi.ac.uk/pdbsum/4p0s PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://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> [[http://www.uniprot.org/uniprot/EME1_HUMAN EME1_HUMAN]] Interacts with MUS81 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:12686547</ref> <ref>PMID:12721304</ref> <ref>PMID:14617801</ref> <ref>PMID:17289582</ref>
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baek, K.]]
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[[Category: Baek, K]]
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[[Category: Cho, Y.]]
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[[Category: Cho, Y]]
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[[Category: Gwon, G H.]]
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[[Category: Gwon, G H]]
[[Category: Hydrolase-dna complex]]
[[Category: Hydrolase-dna complex]]
[[Category: Resolvase]]
[[Category: Resolvase]]

Revision as of 17:07, 24 December 2014

human Mus81-Eme1-3'flap DNA complex

4p0s, resolution 6.00Å

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