3dsc: Difference between revisions
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==Crystal structure of P. furiosus Mre11 DNA synaptic complex== | ==Crystal structure of P. furiosus Mre11 DNA synaptic complex== | ||
<StructureSection load='3dsc' size='340' side='right' caption='[[3dsc]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='3dsc' size='340' side='right'caption='[[3dsc]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3dsc]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3dsc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DSC FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=3dsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dsc OCA], [https://pdbe.org/3dsc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dsc RCSB], [https://www.ebi.ac.uk/pdbsum/3dsc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dsc ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MRE11_PYRFU MRE11_PYRFU] 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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pyrococcus furiosus]] | ||
[[Category: | [[Category: Moncalian G]] | ||
[[Category: | [[Category: Shin DS]] | ||
[[Category: | [[Category: Tainer JA]] | ||
[[Category: | [[Category: Williams RS]] | ||
Latest revision as of 15:52, 30 August 2023
Crystal structure of P. furiosus Mre11 DNA synaptic complexCrystal structure of P. furiosus Mre11 DNA synaptic complex
Structural highlights
FunctionMRE11_PYRFU 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMre11 forms the core of the multifunctional Mre11-Rad50-Nbs1 (MRN) complex that detects DNA double-strand breaks (DSBs), activates the ATM checkpoint kinase, and initiates homologous recombination (HR) repair of DSBs. To define the roles of Mre11 in both DNA bridging and nucleolytic processing during initiation of DSB repair, we combined small-angle X-ray scattering (SAXS) and crystal structures of Pyrococcus furiosus Mre11 dimers bound to DNA with mutational analyses of fission yeast Mre11. The Mre11 dimer adopts a four-lobed U-shaped structure that is critical for proper MRN complex assembly and for binding and aligning DNA ends. Further, mutations blocking Mre11 endonuclease activity impair cell survival after DSB induction without compromising MRN complex assembly or Mre11-dependant recruitment of Ctp1, an HR factor, to DSBs. These results show how Mre11 dimerization and nuclease activities initiate repair of DSBs and collapsed replication forks, as well as provide a molecular foundation for understanding cancer-causing Mre11 mutations in ataxia telangiectasia-like disorder (ATLD). Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair.,Williams RS, Moncalian G, Williams JS, Yamada Y, Limbo O, Shin DS, Groocock LM, Cahill D, Hitomi C, Guenther G, Moiani D, Carney JP, Russell P, Tainer JA Cell. 2008 Oct 3;135(1):97-109. PMID:18854158[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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