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| | ==Hexameric ring of Methanococcus voltae RadA== | | ==Hexameric ring of Methanococcus voltae RadA== |
| - | <StructureSection load='4dc9' size='340' side='right' caption='[[4dc9]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='4dc9' size='340' side='right'caption='[[4dc9]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dc9]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanococcus_voltae Methanococcus voltae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DC9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dc9]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanococcus_voltae Methanococcus voltae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DC9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t4g|1t4g]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">radA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2188 Methanococcus voltae])</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=4dc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dc9 OCA], [https://pdbe.org/4dc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dc9 RCSB], [https://www.ebi.ac.uk/pdbsum/4dc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dc9 ProSAT]</span></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=4dc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dc9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dc9 RCSB], [http://www.ebi.ac.uk/pdbsum/4dc9 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RADA_METVO RADA_METVO]] Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity). | + | [https://www.uniprot.org/uniprot/RADA_METVO RADA_METVO] Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity). |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Archaeal RadA proteins are close homologues of eukaryal Rad51 and DMC1 proteins and are remote homologues of bacterial RecA proteins. For the repair of double-stranded breaks in DNA, these recombinases promote a pivotal strand-exchange reaction between homologous single-stranded and double-stranded DNA substrates. This DNA-repair function also plays a key role in the resistance of cancer cells to chemotherapy and radiotherapy and in the resistance of bacterial cells to antibiotics. A hexameric form of a truncated Methanococcus voltae RadA protein devoid of its small N-terminal domain has been crystallized. The RadA hexamers further assemble into two-ringed assemblies. Similar assemblies can be observed in the crystals of Pyrococcus furiosus RadA and Homo sapiens DMC1. In all of these two-ringed assemblies the DNA-interacting L1 region of each protomer points inward towards the centre, creating a highly positively charged locus. The electrostatic characteristics of the central channels can be utilized in the design of novel recombinase inhibitors.
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| - | Structure of a hexameric form of RadA recombinase from Methanococcus voltae.,Du L, Luo Y Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):511-6. doi:, 10.1107/S1744309112010226. Epub 2012 Apr 20. PMID:22691778<ref>PMID:22691778</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | ==See Also== |
| - | </div>
| + | *[[Resolvase 3D structures|Resolvase 3D structures]] |
| - | == References == | + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Methanococcus voltae]] | | [[Category: Methanococcus voltae]] |
| - | [[Category: Du, L]] | + | [[Category: Du L]] |
| - | [[Category: Luo, Y]] | + | [[Category: Luo Y]] |
| - | [[Category: Dna binding protein]]
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| - | [[Category: Hexamer]]
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| - | [[Category: Homologous recombination]]
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| - | [[Category: Rada]]
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| - | [[Category: Reca]]
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| - | [[Category: Recombinase]]
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