4dc9
From Proteopedia
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| - | [[ | + | ==Hexameric ring of Methanococcus voltae RadA== |
| + | <StructureSection load='4dc9' size='340' side='right' caption='[[4dc9]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == 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> | ||
| + | </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> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t4g|1t4g]]</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'>[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Methanococcus voltae]] | [[Category: Methanococcus voltae]] | ||
| - | [[Category: Du, L | + | [[Category: Du, L]] |
| - | [[Category: Luo, Y | + | [[Category: Luo, Y]] |
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Hexamer]] | [[Category: Hexamer]] | ||
Revision as of 16:16, 9 December 2014
Hexameric ring of Methanococcus voltae RadA
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