4tug: Difference between revisions
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==Crystal structure of MjMre11-DNA2 complex== | |||
<StructureSection load='4tug' size='340' side='right'caption='[[4tug]], [[Resolution|resolution]] 3.55Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4tug]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661] 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=4TUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TUG FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.55Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=4tug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tug OCA], [https://pdbe.org/4tug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tug RCSB], [https://www.ebi.ac.uk/pdbsum/4tug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tug ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Mre11-Rad50-Nbs1 (MRN) complex plays important roles in sensing DNA damage, as well as in resecting and tethering DNA ends, and thus participates in double-strand break repair. An earlier structure of Mre11 bound to a short duplex DNA molecule suggested that each Mre11 in a dimer recognizes one DNA duplex to bridge two DNA ends at a short distance. Here, we provide an alternative DNA recognition model based on the structures of Methanococcus jannaschii Mre11 (MjMre11) bound to longer DNA molecules, which may more accurately reflect a broken chromosome. An extended stretch of B-form DNA asymmetrically runs across the whole dimer, with each end of this DNA molecule being recognized by an individual Mre11 monomer. DNA binding induces rigid-body rotation of the Mre11 dimer, which could facilitate melting of the DNA end and its juxtaposition to an active site of Mre11. The identified Mre11 interface binding DNA duplex ends is structurally conserved and shown to functionally contribute to efficient resection, non-homologous end joining, and tolerance to DNA-damaging agents when other resection enzymes are absent. Together, the structural, biochemical, and genetic findings presented here offer new insights into how Mre11 recognizes damaged DNA and facilitates DNA repair. | |||
DNA end recognition by the Mre11 nuclease dimer: insights into resection and repair of damaged DNA.,Sung S, Li F, Park YB, Kim JS, Kim AK, Song OK, Kim J, Che J, Lee SE, Cho Y EMBO J. 2014 Oct 16;33(20):2422-35. doi: 10.15252/embj.201488299. Epub 2014 Aug, 8. PMID:25107472<ref>PMID:25107472</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4tug" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methanocaldococcus jannaschii DSM 2661]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Cho Y]] | |||
[[Category: Sung S]] | |||
Latest revision as of 03:48, 28 December 2023
Crystal structure of MjMre11-DNA2 complexCrystal structure of MjMre11-DNA2 complex
Structural highlights
FunctionMRE11_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). Publication Abstract from PubMedThe Mre11-Rad50-Nbs1 (MRN) complex plays important roles in sensing DNA damage, as well as in resecting and tethering DNA ends, and thus participates in double-strand break repair. An earlier structure of Mre11 bound to a short duplex DNA molecule suggested that each Mre11 in a dimer recognizes one DNA duplex to bridge two DNA ends at a short distance. Here, we provide an alternative DNA recognition model based on the structures of Methanococcus jannaschii Mre11 (MjMre11) bound to longer DNA molecules, which may more accurately reflect a broken chromosome. An extended stretch of B-form DNA asymmetrically runs across the whole dimer, with each end of this DNA molecule being recognized by an individual Mre11 monomer. DNA binding induces rigid-body rotation of the Mre11 dimer, which could facilitate melting of the DNA end and its juxtaposition to an active site of Mre11. The identified Mre11 interface binding DNA duplex ends is structurally conserved and shown to functionally contribute to efficient resection, non-homologous end joining, and tolerance to DNA-damaging agents when other resection enzymes are absent. Together, the structural, biochemical, and genetic findings presented here offer new insights into how Mre11 recognizes damaged DNA and facilitates DNA repair. DNA end recognition by the Mre11 nuclease dimer: insights into resection and repair of damaged DNA.,Sung S, Li F, Park YB, Kim JS, Kim AK, Song OK, Kim J, Che J, Lee SE, Cho Y EMBO J. 2014 Oct 16;33(20):2422-35. doi: 10.15252/embj.201488299. Epub 2014 Aug, 8. PMID:25107472[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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