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3thn

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Current revision (10:09, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3thn' size='340' side='right'caption='[[3thn]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
<StructureSection load='3thn' size='340' side='right'caption='[[3thn]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3thn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3THN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3thn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3THN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THN FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.811&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tho|3tho]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mre11, TM_1635 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3thn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thn OCA], [https://pdbe.org/3thn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3thn RCSB], [https://www.ebi.ac.uk/pdbsum/3thn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3thn ProSAT]</span></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=3thn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thn OCA], [https://pdbe.org/3thn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3thn RCSB], [https://www.ebi.ac.uk/pdbsum/3thn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3thn ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9X1X0_THEMA Q9X1X0_THEMA]
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DNA double-strand breaks (DSBs) threaten genome stability in all kingdoms of life and are linked to cancerogenic chromosome aberrations in humans. The Mre11:Rad50 (MR) complex is an evolutionarily conserved complex of two Rad50 ATPases and a dimer of the Mre11 nuclease that senses and processes DSBs and tethers DNA for repair. ATP binding and hydrolysis by Rad50 is functionally coupled to DNA-binding and tethering, but also regulates Mre11's nuclease in processing DNA ends. To understand how ATP controls the interaction between Mre11 and Rad50, we determined the crystal structure of Thermotoga maritima (Tm) MR trapped in an ATP/ADP state. ATP binding to Rad50 induces a large structural change from an open form with accessible Mre11 nuclease sites into a closed form. Remarkably, the NBD dimer binds in the Mre11 DNA-binding cleft blocking Mre11's dsDNA-binding sites. An accompanying large swivel of the Rad50 coiled coil domains appears to prepare the coiled coils for DNA tethering. DNA-binding studies show that within the complex, Rad50 likely forms a dsDNA-binding site in response to ATP, while the Mre11 nuclease module retains a ssDNA-binding site. Our results suggest a possible mechanism for ATP-dependent DNA tethering and DSB processing by MR.
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ATP driven structural changes of the bacterial Mre11:Rad50 catalytic head complex.,Mockel C, Lammens K, Schele A, Hopfner KP Nucleic Acids Res. 2011 Sep 21. PMID:21937514<ref>PMID:21937514</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3thn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43589]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lammens, K]]
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[[Category: Thermotoga maritima]]
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[[Category: Moeckel, C]]
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[[Category: Lammens K]]
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[[Category: Dna binding protein]]
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[[Category: Moeckel C]]
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[[Category: Dna break]]
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[[Category: Endodeoxyribonuclease]]
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[[Category: Exodeoxyribonuclease]]
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[[Category: Homologous recombination]]
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[[Category: Hydrolase]]
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Current revision

Crystal structure of Mre11 core with manganese

PDB ID 3thn

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