6G1T
TraN, a repressor of an Enterococcus conjugative type IV secretion system
Summary for 6G1T
| Entry DOI | 10.2210/pdb6g1t/pdb |
| Descriptor | AM32, DNA (34-MER), 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (5 entities in total) |
| Functional Keywords | repressor, protein-dna complex, type iv secretion system, dna binding protein |
| Biological source | Enterococcus faecalis More |
| Total number of polymer chains | 3 |
| Total formula weight | 35545.39 |
| Authors | Goessweiner-Mohr, N.,Kohler, V.,Keller, W. (deposition date: 2018-03-22, release date: 2018-07-25, Last modification date: 2024-01-17) |
| Primary citation | Kohler, V.,Goessweiner-Mohr, N.,Aufschnaiter, A.,Fercher, C.,Probst, I.,Pavkov-Keller, T.,Hunger, K.,Wolinski, H.,Buttner, S.,Grohmann, E.,Keller, W. TraN: A novel repressor of an Enterococcus conjugative type IV secretion system. Nucleic Acids Res., 46:9201-9219, 2018 Cited by PubMed Abstract: The dissemination of multi-resistant bacteria represents an enormous burden on modern healthcare. Plasmid-borne conjugative transfer is the most prevalent mechanism, requiring a type IV secretion system that enables bacteria to spread beneficial traits, such as resistance to last-line antibiotics, among different genera. Inc18 plasmids, like the Gram-positive broad host-range plasmid pIP501, are substantially involved in propagation of vancomycin resistance from Enterococci to methicillin-resistant strains of Staphylococcus aureus. Here, we identified the small cytosolic protein TraN as a repressor of the pIP501-encoded conjugative transfer system, since deletion of traN resulted in upregulation of transfer factors, leading to highly enhanced conjugative transfer. Furthermore, we report the complex structure of TraN with DNA and define the exact sequence of its binding motif. Targeting this protein-DNA interaction might represent a novel therapeutic approach against the spreading of antibiotic resistances. PubMed: 30060171DOI: 10.1093/nar/gky671 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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