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| - | ==RUVA COMPLEXED TO A HOLLIDAY JUNCTION.==
| + | #REDIRECT [[7oa5]] This PDB entry is obsolete and replaced by 7oa5 |
| - | <StructureSection load='1bvs' size='340' side='right' caption='[[1bvs]], [[Resolution|resolution]] 3.00Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[1bvs]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_leprae"_hansen_1880 "bacillus leprae" hansen 1880]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BVS FirstGlance]. <br>
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| - | </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=1bvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvs OCA], [http://pdbe.org/1bvs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bvs RCSB], [http://www.ebi.ac.uk/pdbsum/1bvs PDBsum]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/RUVA_MYCLE RUVA_MYCLE]] 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 (By similarity).
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| - | == Evolutionary Conservation ==
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| - | [[Image:Consurf_key_small.gif|200px|right]]
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| - | Check<jmol>
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| - | <jmolCheckbox>
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| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bv/1bvs_consurf.spt"</scriptWhenChecked>
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| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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| - | <text>to colour the structure by Evolutionary Conservation</text>
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| - | </jmolCheckbox>
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| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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| - | <div style="clear:both"></div>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Holliday junctions occur as intermediates in homologous recombination and DNA repair. In bacteria, resolution of Holliday junctions is accomplished by the RuvABC system, consisting of a junction-specific helicase complex RuvAB, which promotes branch migration, and a junction-specific endonuclease RuvC, which nicks two strands. The crystal structure of a complex between the RuvA protein of M. leprae and a synthetic four-way junction has now been determined. Rather than binding on the open surface of a RuvA tetramer as previously suggested, the DNA is sandwiched between two RuvA tetramers, which form a closed octameric shell, stabilized by a conserved tetramer-tetramer interface. Interactions between the DNA backbone and helix-hairpin-helix motifs from both tetramers suggest a mechanism for strand separation promoted by RuvA.
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| - | Crystal structure of an octameric RuvA-Holliday junction complex.,Roe SM, Barlow T, Brown T, Oram M, Keeley A, Tsaneva IR, Pearl LH Mol Cell. 1998 Sep;2(3):361-72. PMID:9774974<ref>PMID:9774974</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 1bvs" style="background-color:#fffaf0;"></div>
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| - | ==See Also==
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| - | *[[Helicase|Helicase]]
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Bacillus leprae hansen 1880]]
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| - | [[Category: Pearl, L H]]
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| - | [[Category: Roe, S M]]
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| - | [[Category: Branch migration]]
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| - | [[Category: Dna binding protein]]
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| - | [[Category: Dna repair]]
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| - | [[Category: Holliday junction resolvase component]]
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