5f3w: Difference between revisions
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==Structure of the ATPrS-Mre11/Rad50-DNA complex== | |||
<StructureSection load='5f3w' size='340' side='right' caption='[[5f3w]], [[Resolution|resolution]] 3.11Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5f3w]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F3W FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<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=5f3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f3w OCA], [http://pdbe.org/5f3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f3w RCSB], [http://www.ebi.ac.uk/pdbsum/5f3w PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/MRE11_METJA MRE11_METJA]] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity (By similarity). [[http://www.uniprot.org/uniprot/RAD50_METJA RAD50_METJA]] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ATP-dependent DNA end recognition and nucleolytic processing are central functions of the Mre11/Rad50 (MR) complex in DNA double-strand break repair. However, it is still unclear how ATP binding and hydrolysis primes the MR function and regulates repair pathway choice in cells. Here, Methanococcus jannaschii MR-ATPgammaS-DNA structure reveals that the partly deformed DNA runs symmetrically across central groove between two ATPgammaS-bound Rad50 nucleotide-binding domains. Duplex DNA cannot access the Mre11 active site in the ATP-free full-length MR complex. ATP hydrolysis drives rotation of the nucleotide-binding domain and induces the DNA melting so that the substrate DNA can access Mre11. Our findings suggest that the ATP hydrolysis-driven conformational changes in both DNA and the MR complex coordinate the melting and endonuclease activity. | |||
ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex.,Liu Y, Sung S, Kim Y, Li F, Gwon G, Jo A, Kim AK, Kim T, Song OK, Lee SE, Cho Y EMBO J. 2015 Dec 30. pii: e201592462. PMID:26717941<ref>PMID:26717941</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5f3w" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Liu, Y]] | |||
[[Category: Complex]] | |||
[[Category: Dna binding protein-hydrolase-dna complex]] | |||
[[Category: Nuclease]] | |||
Revision as of 15:12, 2 March 2016
Structure of the ATPrS-Mre11/Rad50-DNA complex
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