8rxc | pdb_00008rxc

RadA helicase from Streptococcus pneumoniae coordinating dsDNA

spinqualitylabelsall models 8rxc, resolution 3.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8rxc is a 8 chain structure with sequence from Streptococcus pneumoniae and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.15Å Ligands: AGS, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A237IXT5_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] Publication Abstract from PubMed Some DNA helicases play central and specific roles in genome maintenance and plasticity through their branch migration activity in different pathways of homologous recombination. RadA is a highly conserved bacterial helicase involved in DNA repair throughout all bacterial species. In Gram-positive Firmicutes, it also has a role in natural transformation, while in Gram-negative bacteria, ComM is the canonical transformation-specific helicase. Both RadA and ComM helicases form hexameric rings and use ATP hydrolysis as an energy source to propel themselves along DNA. In this study, we present the cryoEM structures of RadA and ComM interacting with DNA and ATP analogs. These structures reveal important molecular interactions that couple ATP hydrolysis and DNA binding in RadA, as well as the role of the Lon protease-like domain, shared by RadA and ComM, in this process. Taken together, these results provide new molecular insights into the mechanisms of DNA branch migration in different pathways of homologous recombination. Structural insights into the mechanism of DNA branch migration during homologous recombination in bacteria.,Rosa LT, Vernhes E, Soulet AL, Polard P, Fronzes R EMBO J. 2024 Oct 18. doi: 10.1038/s44318-024-00264-5. PMID:39424952 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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