6WIM
CdiB from Escherichia coli
Summary for 6WIM
| Entry DOI | 10.2210/pdb6wim/pdb |
| Descriptor | Outer membrane transporter CdiB, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | membrane protein, transport protein, tpsb, omp85, cdib |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 60294.06 |
| Authors | Guerin, J.,Botos, I.,Buchanan, S.K. (deposition date: 2020-04-10, release date: 2020-11-04, Last modification date: 2024-10-09) |
| Primary citation | Guerin, J.,Botos, I.,Zhang, Z.,Lundquist, K.,Gumbart, J.C.,Buchanan, S.K. Structural insight into toxin secretion by contact dependent growth inhibition transporters. Elife, 9:-, 2020 Cited by PubMed Abstract: Bacterial contact-dependent growth inhibition (CDI) systems use a type Vb secretion mechanism to export large CdiA toxins across the outer membrane by dedicated outer membrane transporters called CdiB. Here, we report the first crystal structures of two CdiB transporters from and . CdiB transporters adopt a TpsB fold, containing a 16-stranded transmembrane β-barrel connected to two periplasmic domains. The lumen of the CdiB pore is occluded by an N-terminal α-helix and the conserved extracellular loop 6; these two elements adopt different conformations in the structures. We identified a conserved DxxG motif located on strand β1 that connects loop 6 through different networks of interactions. Structural modifications of DxxG induce rearrangement of extracellular loops and alter interactions with the N-terminal α-helix, preparing the system for α-helix ejection. Using structural biology, functional assays, and molecular dynamics simulations, we show how the barrel pore is primed for CdiA toxin secretion. PubMed: 33089781DOI: 10.7554/eLife.58100 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report
