2fpm

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(New page: 200px<br /><applet load="2fpm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fpm, resolution 2.00&Aring;" /> '''RadA recombinase in ...)
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[[Image:2fpm.jpg|left|200px]]<br /><applet load="2fpm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2fpm, resolution 2.00&Aring;" />
 
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'''RadA recombinase in complex with AMP-PNP and high concentration of K+'''<br />
 
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==Overview==
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==RadA recombinase in complex with AMP-PNP and high concentration of K+==
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Members of a superfamily of RecA-like recombinases facilitate a central, strand exchange reaction in the DNA repair process. Archaeal RadA and, Rad51 and eukaryal Rad51 and meiosis-specific DMC1 form a closely related, group of recombinases distinct from bacterial RecA. Nevertheless, all such, recombinases share a conserved core domain which carries the ATPase site, and putative DNA-binding sites. Here we present the crystal structure of, an archaeal RadA from Methanococcus voltae (MvRadA) in complex with ADP, and Mg2+ at 2.1 A resolution. The crystallized RadA-ADP filament has an, extended helical pitch similar to those of previously determined, structures in the presence of nonhydrolyzable ATP analogue AMP-PNP., Structural comparison reveals two recurrent conformations with an, extensive allosteric effect spanning the ATPase site and the putative, DNA-binding L2 region. Varied conformations of the L2 region also imply a, dynamic nature of recombinase-bound DNA.
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<StructureSection load='2fpm' size='340' side='right'caption='[[2fpm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2fpm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanococcus_voltae Methanococcus voltae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1z4d 1z4d]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FPM 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&#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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2fpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpm OCA], [https://pdbe.org/2fpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fpm RCSB], [https://www.ebi.ac.uk/pdbsum/2fpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fpm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RADA_METVO RADA_METVO] Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (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/fp/2fpm_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=2fpm 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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Members of a superfamily of RecA-like recombinases facilitate a central strand exchange reaction in the DNA repair process. Archaeal RadA and Rad51 and eukaryal Rad51 and meiosis-specific DMC1 form a closely related group of recombinases distinct from bacterial RecA. Nevertheless, all such recombinases share a conserved core domain which carries the ATPase site and putative DNA-binding sites. Here we present the crystal structure of an archaeal RadA from Methanococcus voltae (MvRadA) in complex with ADP and Mg2+ at 2.1 A resolution. The crystallized RadA-ADP filament has an extended helical pitch similar to those of previously determined structures in the presence of nonhydrolyzable ATP analogue AMP-PNP. Structural comparison reveals two recurrent conformations with an extensive allosteric effect spanning the ATPase site and the putative DNA-binding L2 region. Varied conformations of the L2 region also imply a dynamic nature of recombinase-bound DNA.
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==About this Structure==
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Crystal structure of Methanococcus voltae RadA in complex with ADP: hydrolysis-induced conformational change.,Qian X, Wu Y, He Y, Luo Y Biochemistry. 2005 Oct 25;44(42):13753-61. PMID:16229465<ref>PMID:16229465</ref>
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2FPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanococcus_voltae Methanococcus voltae] with MG, K and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1Z4D. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FPM 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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Crystal structure of Methanococcus voltae RadA in complex with ADP: hydrolysis-induced conformational change., Qian X, Wu Y, He Y, Luo Y, Biochemistry. 2005 Oct 25;44(42):13753-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16229465 16229465]
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</div>
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[[Category: Methanococcus voltae]]
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<div class="pdbe-citations 2fpm" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: He, Y.]]
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[[Category: Luo, Y.]]
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[[Category: Moya, I.A.]]
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[[Category: Qian, X.]]
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[[Category: Wu, Y.]]
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[[Category: ANP]]
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[[Category: K]]
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[[Category: MG]]
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[[Category: atpase]]
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[[Category: co-factors]]
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[[Category: potassium-dependence]]
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[[Category: protein-atp complex]]
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[[Category: rada/adp complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:41:09 2007''
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==See Also==
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*[[Resolvase 3D structures|Resolvase 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: Methanococcus voltae]]
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[[Category: He Y]]
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[[Category: Luo Y]]
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[[Category: Moya IA]]
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[[Category: Qian X]]
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[[Category: Wu Y]]

Current revision

RadA recombinase in complex with AMP-PNP and high concentration of K+

PDB ID 2fpm

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