2h5x

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(New page: 200px<br /><applet load="2h5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h5x, resolution 2.70&Aring;" /> '''RuvA from Mycobacter...)
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[[Image:2h5x.gif|left|200px]]<br /><applet load="2h5x" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2h5x, resolution 2.70&Aring;" />
 
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'''RuvA from Mycobacterium tuberculosis'''<br />
 
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==Overview==
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==RuvA from Mycobacterium tuberculosis==
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The process of recombinational repair is crucial for maintaining genomic, integrity and generating biological diversity. In association with RuvB, and RuvC, RuvA plays a central role in processing and resolving Holliday, junctions, which are a critical intermediate in homologous recombination., Here, the cloning, purification and structure determination of the RuvA, protein from Mycobacterium tuberculosis (MtRuvA) are reported. Analysis of, the structure and comparison with other known RuvA proteins reveal an, octameric state with conserved subunit-subunit interaction surfaces, indicating the requirement of octamer formation for biological activity. A, detailed analysis of plasticity in the RuvA molecules has led to insights, into the invariant and variable regions, thus providing a framework for, understanding regional flexibility in various aspects of RuvA function.
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<StructureSection load='2h5x' size='340' side='right'caption='[[2h5x]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2h5x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H5X FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h5x OCA], [https://pdbe.org/2h5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h5x RCSB], [https://www.ebi.ac.uk/pdbsum/2h5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h5x ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RUVA_MYCTU RUVA_MYCTU] 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/h5/2h5x_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/main_output.php?pdb_ID=2h5x 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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The process of recombinational repair is crucial for maintaining genomic integrity and generating biological diversity. In association with RuvB and RuvC, RuvA plays a central role in processing and resolving Holliday junctions, which are a critical intermediate in homologous recombination. Here, the cloning, purification and structure determination of the RuvA protein from Mycobacterium tuberculosis (MtRuvA) are reported. Analysis of the structure and comparison with other known RuvA proteins reveal an octameric state with conserved subunit-subunit interaction surfaces, indicating the requirement of octamer formation for biological activity. A detailed analysis of plasticity in the RuvA molecules has led to insights into the invariant and variable regions, thus providing a framework for understanding regional flexibility in various aspects of RuvA function.
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==About this Structure==
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Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.,Prabu JR, Thamotharan S, Khanduja JS, Alipio EZ, Kim CY, Waldo GS, Terwilliger TC, Segelke B, Lekin T, Toppani D, Hung LW, Yu M, Bursey E, Muniyappa K, Chandra NR, Vijayan M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):731-4. Epub 2006 Jul 24. PMID:16880543<ref>PMID:16880543</ref>
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2H5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H5X OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination., Prabu JR, Thamotharan S, Khanduja JS, Alipio EZ, Kim CY, Waldo GS, Terwilliger TC, Segelke B, Lekin T, Toppani D, Hung LW, Yu M, Bursey E, Muniyappa K, Chandra NR, Vijayan M, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):731-4. Epub 2006 Jul 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16880543 16880543]
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</div>
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[[Category: Mycobacterium tuberculosis]]
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<div class="pdbe-citations 2h5x" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Alipio, E.Z.]]
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[[Category: Bursey, E.]]
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[[Category: Chandra, N.R.]]
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[[Category: Hung, L.W.]]
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[[Category: Khanduja, J.S.]]
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[[Category: Kim, C.Y.]]
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[[Category: Lekin, T.]]
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[[Category: Muniyappa, K.]]
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[[Category: Prabu, J.R.]]
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[[Category: Segelke, B.]]
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[[Category: Terwilliger, T.C.]]
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[[Category: Thamotharan, S.]]
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[[Category: Toppani, D.]]
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[[Category: Vijayan, M.]]
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[[Category: Waldo, G.S.]]
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[[Category: Yu, M.]]
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[[Category: GOL]]
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[[Category: holliday junction binding]]
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[[Category: recombination]]
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[[Category: ruva]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:33:21 2007''
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==See Also==
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*[[Helicase 3D structures|Helicase 3D structures]]
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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: Large Structures]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Alipio EZ]]
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[[Category: Bursey E]]
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[[Category: Chandra NR]]
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[[Category: Hung LW]]
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[[Category: Khanduja JS]]
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[[Category: Kim CY]]
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[[Category: Lekin T]]
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[[Category: Muniyappa K]]
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[[Category: Prabu JR]]
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[[Category: Segelke B]]
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[[Category: Terwilliger TC]]
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[[Category: Thamotharan S]]
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[[Category: Toppani D]]
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[[Category: Vijayan M]]
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[[Category: Waldo GS]]
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[[Category: Yu M]]

Current revision

RuvA from Mycobacterium tuberculosis

PDB ID 2h5x

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