5LD2
Cryo-EM structure of RecBCD+DNA complex revealing activated nuclease domain
Summary for 5LD2
| Entry DOI | 10.2210/pdb5ld2/pdb |
| EMDB information | 4038 |
| Descriptor | RecBCD enzyme subunit RecB,RecBCD enzyme subunit RecB,RecBCD enzyme subunit RecB, RecBCD enzyme subunit RecC, RecBCD enzyme subunit RecD, ... (6 entities in total) |
| Functional Keywords | helicase, nuclease, sh3, homologous recombination, hydrolase |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 4 |
| Total formula weight | 351710.12 |
| Authors | Wilkinson, M.,Chaban, Y.,Wigley, D.B. (deposition date: 2016-06-23, release date: 2016-10-05, Last modification date: 2024-05-15) |
| Primary citation | Wilkinson, M.,Chaban, Y.,Wigley, D.B. Mechanism for nuclease regulation in RecBCD. Elife, 5:-, 2016 Cited by PubMed Abstract: In bacterial cells, processing of double-stranded DNA breaks for repair by homologous recombination is catalysed by AddAB, AdnAB or RecBCD-type helicase-nucleases. These enzyme complexes are highly processive, duplex unwinding and degrading machines that require tight regulation. Here, we report the structure of E.coli RecBCD, determined by cryoEM at 3.8 Å resolution, with a DNA substrate that reveals how the nuclease activity of the complex is activated once unwinding progresses. Extension of the 5'-tail of the unwound duplex induces a large conformational change in the RecD subunit, that is transferred through the RecC subunit to activate the nuclease domain of the RecB subunit. The process involves a SH3 domain that binds to a region of the RecB subunit in a binding mode that is distinct from others observed previously in SH3 domains and, to our knowledge, this is the first example of peptide-binding of an SH3 domain in a bacterial system. PubMed: 27644322DOI: 10.7554/eLife.18227 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.83 Å) |
Structure validation
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