2ygk: Difference between revisions
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<StructureSection load='2ygk' size='340' side='right'caption='[[2ygk]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2ygk' size='340' side='right'caption='[[2ygk]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ygk]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2ygk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YGK FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id=' | <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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ygk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ygk OCA], [https://pdbe.org/2ygk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ygk RCSB], [https://www.ebi.ac.uk/pdbsum/2ygk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ygk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/NURA_SACS2 NURA_SACS2] Involved in DNA double-strand break (DSB) repair (PubMed:22135300). Acts probably with HerA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Processes linear dsDNA probes with 3' or 5' single-stranded overhangs or blunt ends (PubMed:22135300).[UniProtKB:Q8U1N8]<ref>PMID:22135300</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Saccharolobus solfataricus]] | [[Category: Saccharolobus solfataricus]] | ||
[[Category: Abrams AS]] | |||
[[Category: Abrams | [[Category: Blackwood JK]] | ||
[[Category: Blackwood | [[Category: Maman JD]] | ||
[[Category: Maman | [[Category: Pellegrini L]] | ||
[[Category: Pellegrini | [[Category: Robinson NP]] | ||
[[Category: Robinson | [[Category: Rzechorzek NJ]] | ||
[[Category: Rzechorzek | |||
Latest revision as of 17:04, 1 February 2024
Crystal structure of the NurA nuclease from Sulfolobus solfataricusCrystal structure of the NurA nuclease from Sulfolobus solfataricus
Structural highlights
FunctionNURA_SACS2 Involved in DNA double-strand break (DSB) repair (PubMed:22135300). Acts probably with HerA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Processes linear dsDNA probes with 3' or 5' single-stranded overhangs or blunt ends (PubMed:22135300).[UniProtKB:Q8U1N8][1] Publication Abstract from PubMedHelicase-nuclease systems dedicated to DNA end resection in preparation for homologous recombination (HR) are present in all kingdoms of life. In thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during HR-dependent DNA repair. Here we show that HerA and NurA must interact in a complex with specific subunit stoichiometry to process DNA ends efficiently. We determine crystallographically that NurA folds in a toroidal dimer of intertwined RNaseH-like domains. The central channel of the NurA dimer is too narrow for double-stranded DNA but appears well suited to accommodate one or two strands of an unwound duplex. We map a critical interface of the complex to an exposed hydrophobic epitope of NurA abutting the active site. Based upon the presented evidence, we propose alternative mechanisms of DNA end processing by the HerA-NurA complex. Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex.,Blackwood JK, Rzechorzek NJ, Abrams AS, Maman JD, Pellegrini L, Robinson NP Nucleic Acids Res. 2011 Dec 1. PMID:22135300[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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