3d8a | pdb_00003d8a
Co-crystal structure of TraM-TraD complex.
Structural highlights
Function[TRAM1_ECOLI] Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut in the origin of transfer by TraI, at the nic site. Cooperatively binds 3 regions in the F plasmid oriT locus; 2 are required for autoregulation while the other is required for plasmid transfer. Bends oriT DNA less than 50 degrees. Plasmid specificity is conferred by the TraD-TraM pair.[1] [2] [3] [4] [TRAD1_ECOLI] Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Couples the transferosome to a type IV secretion system. Probably forms a pore through which single-stranded plasmid DNA is transferred to the secretion system. The last 37 residues are important for determining plasmid specificity and transfer efficiency, with additional specificity conferred by the TraD-TraM pair.[5] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedF 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. Structural basis of specific TraD-TraM recognition during F plasmid-mediated bacterial conjugation.,Lu J, Wong JJ, Edwards RA, Manchak J, Frost LS, Glover JN Mol Microbiol. 2008 Oct;70(1):89-99. Epub 2008 Aug 19. PMID:18717787[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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