9vc9

Cryo-EM structure of Shewanella decolorationis ComEC

spinqualitylabelsall models 9vc9, resolution 2.77Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9vc9 is a 1 chain structure with sequence from Shewanella decolorationis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.77Å Ligands: AV0, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Structural basis for DNA processing and membrane translocation by ComEC in natural transformation.,Hirano H, Tsuji N, Chiba S, Nureki O Science. 2026 Apr 16;392(6795):311-316. doi: 10.1126/science.aea3485. Epub 2026 , Apr 16. PMID:41990170 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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