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| | <StructureSection load='4d2i' size='340' side='right'caption='[[4d2i]], [[Resolution|resolution]] 2.84Å' scene=''> | | <StructureSection load='4d2i' size='340' side='right'caption='[[4d2i]], [[Resolution|resolution]] 2.84Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d2i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sacs2 Sacs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D2I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d2i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D2I FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </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> |
| - | <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=4d2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2i OCA], [http://pdbe.org/4d2i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d2i RCSB], [http://www.ebi.ac.uk/pdbsum/4d2i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d2i 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=4d2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2i OCA], [https://pdbe.org/4d2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d2i RCSB], [https://www.ebi.ac.uk/pdbsum/4d2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d2i ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/HERA_SACS2 HERA_SACS2]] Involved in DNA double-strand break (DSB) repair (PubMed:22135300). Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA helicase activity (PubMed:22135300, PubMed:25420454).[UniProtKB:Q8U1P0]<ref>PMID:22135300</ref> <ref>PMID:25420454</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sacs2]] | + | [[Category: Saccharolobus solfataricus P2]] |
| - | [[Category: Blackwood, J K]] | + | [[Category: Blackwood JK]] |
| - | [[Category: Bray, S M]] | + | [[Category: Bray SM]] |
| - | [[Category: Maman, J D]] | + | [[Category: Maman JD]] |
| - | [[Category: Pellegrini, L]] | + | [[Category: Pellegrini L]] |
| - | [[Category: Robinson, N P]] | + | [[Category: Robinson NP]] |
| - | [[Category: Rzechorzek, N J]] | + | [[Category: Rzechorzek NJ]] |
| - | [[Category: Dna]]
| + | |
| - | [[Category: Helicase]]
| + | |
| - | [[Category: Homologous recombination]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mre11]]
| + | |
| - | [[Category: Nura]]
| + | |
| - | [[Category: Rad50]]
| + | |
| - | [[Category: Translocase]]
| + | |
| Structural highlights
Function
[HERA_SACS2] Involved in DNA double-strand break (DSB) repair (PubMed:22135300). Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA helicase activity (PubMed:22135300, PubMed:25420454).[UniProtKB:Q8U1P0][1] [2]
Publication Abstract from PubMed
The HerA ATPase cooperates with the NurA nuclease and the Mre11-Rad50 complex for the repair of double-strand DNA breaks in thermophilic archaea. Here we extend our structural knowledge of this minimal end-resection apparatus by presenting the first crystal structure of hexameric HerA. The full-length structure visualizes at atomic resolution the N-terminal HerA-ATP synthase domain and a conserved C-terminal extension, which acts as a physical brace between adjacent protomers. The brace also interacts in trans with nucleotide-binding residues of the neighbouring subunit. Our observations support a model in which the coaxial interaction of the HerA ring with the toroidal NurA dimer generates a continuous channel traversing the complex. HerA-driven translocation would propel the DNA towards the narrow annulus of NurA, leading to duplex melting and nucleolytic digestion. This system differs substantially from the bacterial end-resection paradigms. Our findings suggest a novel mode of DNA-end processing by this integrated archaeal helicase-nuclease machine.
Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea.,Rzechorzek NJ, Blackwood JK, Bray SM, Maman JD, Pellegrini L, Robinson NP Nat Commun. 2014 Nov 25;5:5506. doi: 10.1038/ncomms6506. PMID:25420454[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Blackwood JK, Rzechorzek NJ, Abrams AS, Maman JD, Pellegrini L, Robinson NP. Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex. Nucleic Acids Res. 2011 Dec 1. PMID:22135300 doi:10.1093/nar/gkr1157
- ↑ Rzechorzek NJ, Blackwood JK, Bray SM, Maman JD, Pellegrini L, Robinson NP. Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea. Nat Commun. 2014 Nov 25;5:5506. doi: 10.1038/ncomms6506. PMID:25420454 doi:http://dx.doi.org/10.1038/ncomms6506
- ↑ Rzechorzek NJ, Blackwood JK, Bray SM, Maman JD, Pellegrini L, Robinson NP. Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea. Nat Commun. 2014 Nov 25;5:5506. doi: 10.1038/ncomms6506. PMID:25420454 doi:http://dx.doi.org/10.1038/ncomms6506
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