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| | <StructureSection load='1c7y' size='340' side='right'caption='[[1c7y]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='1c7y' size='340' side='right'caption='[[1c7y]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1c7y]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C7Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1c7y]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C7Y FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hjp|1hjp]]</div></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]] 3.1Å</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=1c7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c7y OCA], [https://pdbe.org/1c7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c7y RCSB], [https://www.ebi.ac.uk/pdbsum/1c7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c7y 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=1c7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c7y OCA], [https://pdbe.org/1c7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c7y RCSB], [https://www.ebi.ac.uk/pdbsum/1c7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c7y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RUVA_ECOLI RUVA_ECOLI]] The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. Binds both single- and double-stranded DNA (dsDNA). Binds preferentially to supercoiled rather than to relaxed dsDNA.<ref>PMID:8433990</ref>
| + | [https://www.uniprot.org/uniprot/RUVA_ECOLI RUVA_ECOLI] The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. Binds both single- and double-stranded DNA (dsDNA). Binds preferentially to supercoiled rather than to relaxed dsDNA.<ref>PMID:8433990</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ariyoshi, M]] | + | [[Category: Ariyoshi M]] |
| - | [[Category: Iwasaki, H]] | + | [[Category: Iwasaki H]] |
| - | [[Category: Morikawa, K]] | + | [[Category: Morikawa K]] |
| - | [[Category: Nishino, T]] | + | [[Category: Nishino T]] |
| - | [[Category: Shinagawa, H]] | + | [[Category: Shinagawa H]] |
| - | [[Category: Helix-hairpin-helix]]
| + | |
| - | [[Category: Holliday junction]]
| + | |
| - | [[Category: Homologous recombination]]
| + | |
| - | [[Category: Protein-dna complex]]
| + | |
| - | [[Category: Recombination-dna complex]]
| + | |
| Structural highlights
Function
RUVA_ECOLI The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. Binds both single- and double-stranded DNA (dsDNA). Binds preferentially to supercoiled rather than to relaxed dsDNA.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In the major pathway of homologous DNA recombination in prokaryotic cells, the Holliday junction intermediate is processed through its association with RuvA, RuvB, and RuvC proteins. Specific binding of the RuvA tetramer to the Holliday junction is required for the RuvB motor protein to be loaded onto the junction DNA, and the RuvAB complex drives the ATP-dependent branch migration. We solved the crystal structure of the Holliday junction bound to a single Escherichia coli RuvA tetramer at 3.1-A resolution. In this complex, one side of DNA is accessible for cleavage by RuvC resolvase at the junction center. The refined junction DNA structure revealed an open concave architecture with a four-fold symmetry. Each arm, with B-form DNA, in the Holliday junction is predominantly recognized in the minor groove through hydrogen bonds with two repeated helix-hairpin-helix motifs of each RuvA subunit. The local conformation near the crossover point, where two base pairs are disrupted, suggests a possible scheme for successive base pair rearrangements, which may account for smooth Holliday junction movement without segmental unwinding.
Crystal structure of the holliday junction DNA in complex with a single RuvA tetramer.,Ariyoshi M, Nishino T, Iwasaki H, Shinagawa H, Morikawa K Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8257-62. PMID:10890893[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tsaneva IR, Muller B, West SC. RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro. Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1315-9. PMID:8433990
- ↑ Ariyoshi M, Nishino T, Iwasaki H, Shinagawa H, Morikawa K. Crystal structure of the holliday junction DNA in complex with a single RuvA tetramer. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8257-62. PMID:10890893 doi:10.1073/pnas.140212997
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