9TUD
CryoEM structure of DruH from Druantia type III
Summary for 9TUD
| Entry DOI | 10.2210/pdb9tud/pdb |
| EMDB information | 56257 |
| Descriptor | DruH (1 entity in total) |
| Functional Keywords | immunity, druantia type iii, immunoglobulin, unknown function |
| Biological source | Escherichia coli O157:H7 str. EDL933 |
| Total number of polymer chains | 1 |
| Total formula weight | 127795.68 |
| Authors | Grass, L.M.,Himpich, S.,Hilal, T.,Loll, B.,Wahl, M.C. (deposition date: 2026-01-08, release date: 2026-08-26, Last modification date: 2026-09-30) |
| Primary citation | Himpich, S.,Gaudin, T.,Grass, L.M.,Li, H.,Van Loi, V.,Chen, C.,Klauck, E.,Popp, P.F.,Feussner, M.,Kuropka, B.,Hilal, T.,Loll, B.,Erhardt, M.,Antelmann, H.,Beisel, C.L.,Wahl, M.C. A compact Druantia defense clears phage infections via single-stranded DNA recognition and directional duplex unwinding. Cell Rep, 45:118021-118021, 2026 Cited by PubMed Abstract: Bacteria encode diverse anti-phage defense systems triggered by invader-specific molecular cues. Here, we report that the compact type III-A Druantia system recognizes exposed single-stranded DNA to block phage replication and drive phage clearance. Using representative systems from Escherichia coli, we show that the two encoded proteins, DruE and DruH, together clear restriction-sensitive or recombination-prone phages without affecting cell growth or viability. DruE dimerizes and engages DNA at exposed single-stranded regions to unwind DNA with 3'-to-5' directionality, resorting to unique molecular lock, wedge, and clamp elements that aid strand separation and processive translocation. DruH is a monomer in isolation and indirectly interacts with DruE and other host proteins under uninfected conditions, with an infection resulting in the dissociation of the complex. Taken together, our results reveal that exposed single-stranded DNA can trigger bacterial immunity through the directional helicase activity of type III-A Druantia. PubMed: 42771523DOI: 10.1016/j.celrep.2026.118021 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
Download full validation report
