3taz

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<StructureSection load='3taz' size='340' side='right'caption='[[3taz]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='3taz' size='340' side='right'caption='[[3taz]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3taz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TAZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3taz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TAZ 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 3.2&#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;'>[[3tai|3tai]], [[3tal|3tal]]</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF1168 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</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=3taz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3taz OCA], [https://pdbe.org/3taz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3taz RCSB], [https://www.ebi.ac.uk/pdbsum/3taz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3taz 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=3taz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3taz OCA], [https://pdbe.org/3taz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3taz RCSB], [https://www.ebi.ac.uk/pdbsum/3taz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3taz 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/NURA_PYRFU NURA_PYRFU] Involved in DNA double-strand break (DSB) repair (PubMed:18957200). Acts probably with HerA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (PubMed:18957200). Exhibits 5' endonuclease activity and both 5' and 3' exonuclease activities (PubMed:22064858).<ref>PMID:18957200</ref> <ref>PMID:22064858</ref>
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Generation of the 3' overhang is a critical event during homologous recombination (HR) repair of DNA double strand breaks. A 5'-3' nuclease, NurA, plays an important role in generating 3' single-stranded DNA during archaeal HR, together with Mre11-Rad50 and HerA. We have determined the crystal structures of apo- and dAMP-Mn(2)(+)-bound NurA from Pyrococcus furiousus (Pf NurA) to provide the basis for its cleavage mechanism. Pf NurA forms a pyramid-shaped dimer containing a large central channel on one side, which becomes narrower towards the peak of the pyramid. The structure contains a PIWI domain with high similarity to argonaute, endoV nuclease and RNase H. The two active sites, each of which contains Mn(2)(+) ion(s) and dAMP, are at the corners of the elliptical channel near the flat face of the dimer. The 3' OH group of the ribose ring is directed toward the channel entrance, explaining the 5'-3' nuclease activity of Pf NurA. We provide a DNA binding and cleavage model for Pf NurA.
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Crystal structure of the NurA-dAMP-Mn2+ complex.,Chae J, Kim YC, Cho Y Nucleic Acids Res. 2011 Nov 7. PMID:22064858<ref>PMID:22064858</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 3taz" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pyrfu]]
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[[Category: Pyrococcus furiosus DSM 3638]]
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[[Category: Chae, J]]
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[[Category: Chae J]]
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[[Category: Cho, Y]]
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[[Category: Cho Y]]
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[[Category: Kim, Y C]]
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[[Category: Kim YC]]
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[[Category: Hydrolase]]
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[[Category: Recombination]]
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Revision as of 08:37, 20 March 2024

Crystal structure of NurA bound to dAMP and manganese

PDB ID 3taz

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