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5dny

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==Structure of the ATPrS-Mre11/Rad50-DNA complex==
==Structure of the ATPrS-Mre11/Rad50-DNA complex==
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<StructureSection load='5dny' size='340' side='right' caption='[[5dny]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
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<StructureSection load='5dny' size='340' side='right'caption='[[5dny]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5dny]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DNY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DNY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5dny]] is a 6 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=5DNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DNY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</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]] 3.11&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dny OCA], [http://pdbe.org/5dny PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dny RCSB], [http://www.ebi.ac.uk/pdbsum/5dny PDBsum]</span></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=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5dny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dny OCA], [https://pdbe.org/5dny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dny RCSB], [https://www.ebi.ac.uk/pdbsum/5dny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dny ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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). [[http://www.uniprot.org/uniprot/RAD50_METJA RAD50_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. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449]
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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ATP-dependent DNA end recognition and nucleolytic processing are central functions of the Mre11/Rad50 (MR) complex in DNA double-strand break repair. However, it is still unclear how ATP binding and hydrolysis primes the MR function and regulates repair pathway choice in cells. Here, Methanococcus jannaschii MR-ATPgammaS-DNA structure reveals that the partly deformed DNA runs symmetrically across central groove between two ATPgammaS-bound Rad50 nucleotide-binding domains. Duplex DNA cannot access the Mre11 active site in the ATP-free full-length MR complex. ATP hydrolysis drives rotation of the nucleotide-binding domain and induces the DNA melting so that the substrate DNA can access Mre11. Our findings suggest that the ATP hydrolysis-driven conformational changes in both DNA and the MR complex coordinate the melting and endonuclease activity.
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ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex.,Liu Y, Sung S, Kim Y, Li F, Gwon G, Jo A, Kim AK, Kim T, Song OK, Lee SE, Cho Y EMBO J. 2015 Dec 30. pii: e201592462. PMID:26717941<ref>PMID:26717941</ref>
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==See Also==
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*[[ATPase 3D structures|ATPase 3D structures]]
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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 5dny" 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: Liu, Y]]
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[[Category: Large Structures]]
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[[Category: Nuclease]]
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[[Category: Methanocaldococcus jannaschii DSM 2661]]
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[[Category: Recombination-dna complex]]
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[[Category: Synthetic construct]]
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[[Category: Liu Y]]

Current revision

Structure of the ATPrS-Mre11/Rad50-DNA complex

PDB ID 5dny

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