3qf7

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Current revision (10:47, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3qf7' size='340' side='right'caption='[[3qf7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3qf7' size='340' side='right'caption='[[3qf7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qf7]] is a 4 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=3QF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QF7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qf7]] is a 4 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=3QF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QF7 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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.9&#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;'>[[3qg5|3qg5]]</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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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'>[https://proteopedia.org/fgij/fg.htm?mol=3qf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qf7 OCA], [https://pdbe.org/3qf7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qf7 RCSB], [https://www.ebi.ac.uk/pdbsum/3qf7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qf7 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=3qf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qf7 OCA], [https://pdbe.org/3qf7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qf7 RCSB], [https://www.ebi.ac.uk/pdbsum/3qf7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qf7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/RAD50_THEMA RAD50_THEMA]] 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 (By similarity).
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[https://www.uniprot.org/uniprot/RAD50_THEMA RAD50_THEMA] 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 (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The MR (Mre11 nuclease and Rad50 ABC ATPase) complex is an evolutionarily conserved sensor for DNA double-strand breaks, highly genotoxic lesions linked to cancer development. MR can recognize and process DNA ends even if they are blocked and misfolded. To reveal its mechanism, we determined the crystal structure of the catalytic head of Thermotoga maritima MR and analyzed ATP-dependent conformational changes. MR adopts an open form with a central Mre11 nuclease dimer and two peripheral Rad50 molecules, a form suited for sensing obstructed breaks. The Mre11 C-terminal helix-loop-helix domain binds Rad50 and attaches flexibly to the nuclease domain, enabling large conformational changes. ATP binding to the two Rad50 subunits induces a rotation of the Mre11 helix-loop-helix and Rad50 coiled-coil domains, creating a clamp conformation with increased DNA-binding activity. The results suggest that MR is an ATP-controlled transient molecular clamp at DNA double-strand breaks. PAPERFLICK:
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The Mre11:Rad50 Structure Shows an ATP-Dependent Molecular Clamp in DNA Double-Strand Break Repair.,Lammens K, Bemeleit DJ, Mockel C, Clausing E, Schele A, Hartung S, Schiller CB, Lucas M, Angermuller C, Soding J, Strasser K, Hopfner KP Cell. 2011 Apr 1;145(1):54-66. PMID:21458667<ref>PMID:21458667</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 3qf7" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
*[[ATPase 3D structures|ATPase 3D structures]]
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== References ==
 
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<references/>
 
__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: Abc-atpase]]
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[[Category: Moeckel C]]
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[[Category: Atpase]]
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[[Category: Hydrolase]]
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[[Category: Mre11]]
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Current revision

The Mre11:Rad50 complex forms an ATP dependent molecular clamp in DNA double-strand break repair

PDB ID 3qf7

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