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| | <StructureSection load='5lkq' size='340' side='right'caption='[[5lkq]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5lkq' size='340' side='right'caption='[[5lkq]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lkq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LKQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LKQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lkq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LKQ FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lkq OCA], [http://pdbe.org/5lkq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lkq RCSB], [http://www.ebi.ac.uk/pdbsum/5lkq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lkq ProSAT]</span></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]] 2.498Å</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=5lkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lkq OCA], [https://pdbe.org/5lkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lkq RCSB], [https://www.ebi.ac.uk/pdbsum/5lkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lkq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A0T7K9X0_STREE A0A0T7K9X0_STREE]] DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.[RuleBase:RU003555] Plays a role in repairing double-strand DNA breaks, probably involving stabilizing or processing branched DNA or blocked replication forks.[HAMAP-Rule:MF_01498] | + | [https://www.uniprot.org/uniprot/RADA_STRR6 RADA_STRR6] Plays a role in repairing double-strand DNA breaks, probably involving stabilizing or processing branched DNA or blocked replication forks (By similarity). Required for efficient transformation with chromosomal (linear) DNA, but not for replicative plasmid DNA. Its increased sensitivity to a DNA damaging agent suggests it may be required for DNA repair (PubMed:17631629).[HAMAP-Rule:MF_01498]<ref>PMID:17631629</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fronzes, R]] | + | [[Category: Streptococcus pneumoniae]] |
| - | [[Category: Rapisarda, C]] | + | [[Category: Fronzes R]] |
| - | [[Category: Dna-binding]] | + | [[Category: Rapisarda C]] |
| - | [[Category: Helicase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lon-protease]]
| + | |
| - | [[Category: Recombination]]
| + | |
| Structural highlights
Function
RADA_STRR6 Plays a role in repairing double-strand DNA breaks, probably involving stabilizing or processing branched DNA or blocked replication forks (By similarity). Required for efficient transformation with chromosomal (linear) DNA, but not for replicative plasmid DNA. Its increased sensitivity to a DNA damaging agent suggests it may be required for DNA repair (PubMed:17631629).[HAMAP-Rule:MF_01498][1]
Publication Abstract from PubMed
Homologous recombination (HR) is a central process of genome biology driven by a conserved recombinase, which catalyses the pairing of single-stranded DNA (ssDNA) with double-stranded DNA to generate a D-loop intermediate. Bacterial RadA is a conserved HR effector acting with RecA recombinase to promote ssDNA integration. The mechanism of this RadA-mediated assistance to RecA is unknown. Here, we report functional and structural analyses of RadA from the human pathogen Streptococcus pneumoniae. RadA is found to facilitate RecA-driven ssDNA recombination over long genomic distances during natural transformation. RadA is revealed as a hexameric DnaB-type helicase, which interacts with RecA to promote orientated unwinding of branched DNA molecules mimicking D-loop boundaries. These findings support a model of DNA branch migration in HR, relying on RecA-mediated loading of RadA hexamers on each strand of the recipient dsDNA in the D-loop, from which they migrate divergently to facilitate incorporation of invading ssDNA.
Bacterial RadA is a DnaB-type helicase interacting with RecA to promote bidirectional D-loop extension.,Marie L, Rapisarda C, Morales V, Berge M, Perry T, Soulet AL, Gruget C, Remaut H, Fronzes R, Polard P Nat Commun. 2017 May 31;8:15638. doi: 10.1038/ncomms15638. PMID:28561029[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Burghout P, Bootsma HJ, Kloosterman TG, Bijlsma JJ, de Jongh CE, Kuipers OP, Hermans PW. Search for genes essential for pneumococcal transformation: the RADA DNA repair protein plays a role in genomic recombination of donor DNA. J Bacteriol. 2007 Sep;189(18):6540-50. PMID:17631629 doi:10.1128/JB.00573-07
- ↑ Marie L, Rapisarda C, Morales V, Berge M, Perry T, Soulet AL, Gruget C, Remaut H, Fronzes R, Polard P. Bacterial RadA is a DnaB-type helicase interacting with RecA to promote bidirectional D-loop extension. Nat Commun. 2017 May 31;8:15638. doi: 10.1038/ncomms15638. PMID:28561029 doi:http://dx.doi.org/10.1038/ncomms15638
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