2rpe
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2rpe is ON HOLD until Paper Publication Authors: Masuda, T., Ito, Y., Shibata, T., Mikawa, T. Description: hsRad51-bound ssDNA ''Page seeded by [...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==hsRad51-bound ssDNA== | |
| + | <StructureSection load='2rpe' size='340' side='right'caption='[[2rpe]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2rpe]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RPE FirstGlance]. <br> | ||
| + | </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=2rpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rpe OCA], [https://pdbe.org/2rpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rpe RCSB], [https://www.ebi.ac.uk/pdbsum/2rpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rpe ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Homologous recombination, which is critical to genetic diversity, depends on homologous pairing (HP). HP is the switch from parental to recombinant base pairs, which requires expansion of inter-base pair spaces. This expansion unavoidably causes untwisting of the parental double-stranded DNA. RecA/Rad51-catalyzed ATP-dependent HP is extensively stimulated in vitro by negative supercoils, which compensates for untwisting. However, in vivo, double-stranded DNA is relaxed by bound proteins and thus is an unfavorable substrate for RecA/Rad51. In contrast, Mhr1, an ATP-independent HP protein required for yeast mitochondrial homologous recombination, catalyzes HP without the net untwisting of double-stranded DNA. Therefore, we questioned whether Mhr1 uses a novel strategy to promote HP. Here, we found that, like RecA, Mhr1 induced the extension of bound single-stranded DNA. In addition, this structure was induced by all evolutionarily and structurally distinct HP proteins so far tested, including bacterial RecO, viral RecT, and human Rad51. Thus, HP includes the common non-canonical DNA structure and uses a common core mechanism, independent of the species of HP proteins. We discuss the significance of multiple types of HP proteins. | ||
| - | + | A non-canonical DNA structure enables homologous recombination in various genetic systems.,Masuda T, Ito Y, Terada T, Shibata T, Mikawa T J Biol Chem. 2009 Oct 30;284(44):30230-9. Epub 2009 Sep 3. PMID:19729448<ref>PMID:19729448</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2rpe" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ito Y]] | ||
| + | [[Category: Masuda T]] | ||
| + | [[Category: Mikawa T]] | ||
| + | [[Category: Shibata T]] | ||
Current revision
hsRad51-bound ssDNA
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Categories: Large Structures | Ito Y | Masuda T | Mikawa T | Shibata T
