6s85: Difference between revisions

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New page: '''Unreleased structure''' The entry 6s85 is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 6s85 is ON HOLD
==Cutting state of the E. coli Mre11-Rad50 (SbcCD) head complex bound to ADP and dsDNA.==
<SX load='6s85' size='340' side='right' viewer='molstar' caption='[[6s85]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6s85]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S85 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=6s85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s85 OCA], [https://pdbe.org/6s85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s85 RCSB], [https://www.ebi.ac.uk/pdbsum/6s85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s85 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SBCC_ECOLI SBCC_ECOLI] SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity.
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== Publication Abstract from PubMed ==
DNA double-strand breaks (DSBs) threaten genome stability throughout life and are linked to tumorigenesis in humans. To initiate DSB repair by end joining or homologous recombination, the Mre11-nuclease Rad50-ATPase complex detects and processes diverse and obstructed DNA ends, but a structural mechanism is still lacking. Here we report cryo-EM structures of the E. coli Mre11-Rad50 homolog SbcCD in resting and DNA-bound cutting states. In the resting state, Mre11's nuclease is blocked by ATP-Rad50, and the Rad50 coiled coils appear flexible. Upon DNA binding, the two coiled coils zip up into a rod and, together with the Rad50 nucleotide-binding domains, form a clamp around dsDNA. Mre11 moves to the side of Rad50, binds the DNA end, and assembles a DNA cutting channel for the nuclease reactions. The structures reveal how Mre11-Rad50 can detect and process diverse DNA ends and uncover a clamping and gating function for the coiled coils.


Authors:  
Mechanism of DNA End Sensing and Processing by the Mre11-Rad50 Complex.,Kashammer L, Saathoff JH, Lammens K, Gut F, Bartho J, Alt A, Kessler B, Hopfner KP Mol Cell. 2019 Nov 7;76(3):382-394.e6. doi: 10.1016/j.molcel.2019.07.035. Epub, 2019 Sep 3. PMID:31492634<ref>PMID:31492634</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
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<div class="pdbe-citations 6s85" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</SX>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Alt A]]
[[Category: Bartho J]]
[[Category: Gut F]]
[[Category: Hopfner KP]]
[[Category: Kaeshammer L]]
[[Category: Kessler B]]
[[Category: Lammens K]]
[[Category: Saathoff JH]]