9VC6
Cryo-EM structure of Bacillus halodurans ComEC
Summary for 9VC6
| Entry DOI | 10.2210/pdb9vc6/pdb |
| Related | 9VC9 9VCB 9VCF |
| EMDB information | 64944 |
| Descriptor | Competence protein ComEC, Lauryl Maltose Neopentyl Glycol, ZINC ION (3 entities in total) |
| Functional Keywords | competence, dna channel, membrane protein, hydrolase |
| Biological source | Halalkalibacterium halodurans C-125 |
| Total number of polymer chains | 1 |
| Total formula weight | 95514.96 |
| Authors | |
| Primary citation | Hirano, H.,Tsuji, N.,Chiba, S.,Nureki, O. Structural basis for DNA processing and membrane translocation by ComEC in natural transformation. Science, 392:311-316, 2026 Cited by PubMed Abstract: Natural transformation is one of the major pathways of horizontal gene transfer in bacteria, enabling the acquisition of extracellular DNA and its integration into the host genome. ComEC is a membrane protein responsible for DNA translocation in this process, yet its precise function and structure have remained elusive. Here, we report cryo-electron microscopy structures of ComEC in DNA-free, single-stranded DNA (ssDNA)-bound, and double-stranded DNA (dsDNA)-bound forms, together with biochemical analyses. These structures reveal that ComEC cleaves one strand of dsDNA at its extracellular domain and guides the remaining strand into a positively charged pore formed within the membrane domain. These findings provide a structural basis for the long-hypothesized roles of ComEC in both DNA processing and translocation across the inner membrane during natural transformation. PubMed: 41990170DOI: 10.1126/science.aea3485 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.71 Å) |
Structure validation
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