4p0r: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==human Mus81-Eme1-3'flap DNA complex==

== Structural highlights ==

<table><tr><td colspan='2'>[[4p0r]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P0R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P0R FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p0p|4p0p]], [[4p0q|4p0q]], [[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=4p0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p0r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p0r RCSB], [http://www.ebi.ac.uk/pdbsum/4p0r PDBsum]</span></td></tr>

<table>

== 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.

~~The entry 4p0r is ON HOLD until Paper Publication~~

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>

~~Authors: Gwon~~, G.H., Baek, K., Cho, Y.

From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>

</div>

~~Description~~: Resolvase ~~and DNA interation complex~~

== References ==

__TOC__

</StructureSection>

[[Category: Baek, K.]]

[[Category: Cho, Y.]]

[[Category: Gwon, G H.]]

[[Category: Hydrolase-dna complex]]

[[Category: Resolvase]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==human Mus81-Eme1-3'flap DNA complex==
+<StructureSection load='4p0r' size='340' side='right' caption='[[4p0r]], [[Resolution|resolution]] 6.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4p0r]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P0R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P0R FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p0p|4p0p]], [[4p0q|4p0q]], [[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=4p0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p0r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p0r RCSB], [http://www.ebi.ac.uk/pdbsum/4p0r 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.
-The entry 4p0r is ON HOLD  until Paper Publication
+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>
-Authors: Gwon, G.H., Baek, K., Cho, Y.
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Resolvase and DNA interation complex
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Baek, K.]]
+[[Category: Cho, Y.]]
+[[Category: Gwon, G H.]]
+[[Category: Hydrolase-dna complex]]
+[[Category: Resolvase]]