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3tho
From Proteopedia
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| - | [[Image:3tho.png|left|200px]] | ||
| - | < | + | ==Crystal structure of Mre11:Rad50 in its ATP/ADP bound state== |
| - | + | <StructureSection load='3tho' size='340' side='right'caption='[[3tho]], [[Resolution|resolution]] 2.61Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3tho]] is a 2 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=3THO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THO FirstGlance]. <br> | |
| - | + | </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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | -- | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3thn|3thn]]</div></td></tr> |
| - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rad50, TM_1636 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589]), TM_1635 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=3tho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tho OCA], [https://pdbe.org/3tho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tho RCSB], [https://www.ebi.ac.uk/pdbsum/3tho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tho ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3tho" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Atcc 43589]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Lammens, K]] | |
| - | == | + | [[Category: Moeckel, C]] |
| - | < | + | |
| - | [[Category: | + | |
| - | [[Category: Lammens, K | + | |
| - | [[Category: Moeckel, C | + | |
[[Category: Abc atpase]] | [[Category: Abc atpase]] | ||
[[Category: Adenosine triphosphate]] | [[Category: Adenosine triphosphate]] | ||
Current revision
Crystal structure of Mre11:Rad50 in its ATP/ADP bound state
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Categories: Atcc 43589 | Large Structures | Lammens, K | Moeckel, C | Abc atpase | Adenosine triphosphate | Bacterial protein | Dna break | Dna repair | Dna repair enzyme | Dna-binding protein | Double-stranded | Endodeoxyribonuclease | Exodeoxyribonuclease | Hydrolase | Hydrolase-dna binding protein complex | Model | Molecular | Nuclease | Scattering | Small angle | Thermotoga maritima
