2fpk: Difference between revisions
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==RadA recombinase in complex with ADP== | ==RadA recombinase in complex with ADP== | ||
<StructureSection load='2fpk' size='340' side='right' caption='[[2fpk]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2fpk' size='340' side='right' caption='[[2fpk]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fpl|2fpl]], [[2fpm|2fpm]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fpl|2fpl]], [[2fpm|2fpm]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RADA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2188 ATCC 33273])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RADA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2188 ATCC 33273])</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=2fpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpk OCA], [http://pdbe.org/2fpk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fpk RCSB], [http://www.ebi.ac.uk/pdbsum/2fpk PDBsum]</span></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=2fpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpk OCA], [http://pdbe.org/2fpk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fpk RCSB], [http://www.ebi.ac.uk/pdbsum/2fpk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fpk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2fpk" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2fpk" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 10:42, 18 October 2017
RadA recombinase in complex with ADPRadA recombinase in complex with ADP
Structural highlights
Function[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). 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 PubMedMembers 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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