3D8A
Co-crystal structure of TraM-TraD complex.
Summary for 3D8A
| Entry DOI | 10.2210/pdb3d8a/pdb |
| Related | 2G7O |
| Descriptor | Relaxosome protein TraM, Protein traD (3 entities in total) |
| Functional Keywords | tram tetramerization domain, trad c-terminal peptide, protein complex, conjugation, dna-binding, atp-binding, inner membrane, membrane, nucleotide-binding, transmembrane, dna binding protein |
| Biological source | Escherichia coli (strain K12) More |
| Cellular location | Cytoplasm : P10026 |
| Total number of polymer chains | 16 |
| Total formula weight | 72479.42 |
| Authors | Glover, J.N.M.,Lu, J.,Wong, J.J.,Edwards, R.A. (deposition date: 2008-05-22, release date: 2008-09-09, Last modification date: 2023-08-30) |
| Primary citation | Lu, J.,Wong, J.J.,Edwards, R.A.,Manchak, J.,Frost, L.S.,Glover, J.N. Structural basis of specific TraD-TraM recognition during F plasmid-mediated bacterial conjugation. Mol.Microbiol., 70:89-99, 2008 Cited by PubMed Abstract: F plasmid-mediated bacterial conjugation requires interactions between a relaxosome component, TraM, and the coupling protein TraD, a hexameric ring ATPase that forms the cytoplasmic face of the conjugative pore. Here we present the crystal structure of the C-terminal tail of TraD bound to the TraM tetramerization domain, the first structural evidence of relaxosome-coupling protein interactions. The structure reveals the TraD C-terminal peptide bound to each of four symmetry-related grooves on the surface of the TraM tetramer. Extensive protein-protein interactions were observed between the two proteins. Mutational analysis indicates that these interactions are specific and required for efficient F conjugation in vivo. Our results suggest that specific interactions between the C-terminal tail of TraD and the TraM tetramerization domain might lead to more generalized interactions that stabilize the relaxosome-coupling protein complex in preparation for conjugative DNA transfer. PubMed: 18717787DOI: 10.1111/j.1365-2958.2008.06391.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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