6T2V
Cryo-EM structure of the RecBCD in complex with Chi-plus2 substrate
Summary for 6T2V
| Entry DOI | 10.2210/pdb6t2v/pdb |
| EMDB information | 10214 10215 10216 10217 10370 |
| Descriptor | RecBCD enzyme subunit RecB, RecBCD enzyme subunit RecC, RecBCD enzyme subunit RecD, ... (4 entities in total) |
| Functional Keywords | dna repair, homologous recombination, atp hydrolysis, helicase, nuclease, translocation, hydrolase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 356856.20 |
| Authors | Cheng, K.,Wilkinson, M.,Wigley, D.B. (deposition date: 2019-10-09, release date: 2020-01-01, Last modification date: 2024-05-22) |
| Primary citation | Cheng, K.,Wilkinson, M.,Chaban, Y.,Wigley, D.B. A conformational switch in response to Chi converts RecBCD from phage destruction to DNA repair. Nat.Struct.Mol.Biol., 27:71-77, 2020 Cited by PubMed Abstract: The RecBCD complex plays key roles in phage DNA degradation, CRISPR array acquisition (adaptation) and host DNA repair. The switch between these roles is regulated by a DNA sequence called Chi. We report cryo-EM structures of the Escherichia coli RecBCD complex bound to several different DNA forks containing a Chi sequence, including one in which Chi is recognized and others in which it is not. The Chi-recognized structure shows conformational changes in regions of the protein that contact Chi and reveals a tortuous path taken by the DNA. Sequence specificity arises from interactions with both the RecC subunit and the sequence itself. These structures provide molecular details for how Chi is recognized and insights into the changes that occur in response to Chi binding that switch RecBCD from bacteriophage destruction and CRISPR spacer acquisition to constructive host DNA repair. PubMed: 31907455DOI: 10.1038/s41594-019-0355-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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