5vfx

Structure of an accessory protein of the pCW3 relaxosome in complex with the origin of transfer (oriT) DNA

spinqualitylabelsall models 5vfx, resolution 2.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vfx is a 16 chain structure with sequence from Clostridium perfringens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.81Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q1PLI2_CLOPF Publication Abstract from PubMed Conjugation is fundamental for the acquisition of new genetic traits and the development of antibiotic resistance in pathogenic organisms. Here, we show that a hypothetical Clostridium perfringens protein, TcpK, which is encoded by the tetracycline resistance plasmid pCW3, is essential for efficient conjugative DNA transfer. Our studies reveal that TcpK is a member of the winged helix-turn-helix (wHTH) transcription factor superfamily and that it forms a dimer in solution. Furthermore, TcpK specifically binds to a nine-nucleotide sequence that is present as tandem repeats within the pCW3 origin of transfer (oriT). The X-ray crystal structure of the TcpK-TcpK box complex reveals a binding mode centered on and around the beta-wing, which is different from what has been previously shown for other wHTH proteins. Structure-guided mutagenesis experiments validate the specific interaction between TcpK and the DNA molecule. Additional studies highlight that the TcpK dimer is important for specific DNA binding. Crystal structure of TcpK in complex with oriT DNA of the antibiotic resistance plasmid pCW3.,Traore DAK, Wisniewski JA, Flanigan SF, Conroy PJ, Panjikar S, Mok YF, Lao C, Griffin MDW, Adams V, Rood JI, Whisstock JC Nat Commun. 2018 Sep 13;9(1):3732. doi: 10.1038/s41467-018-06096-2. PMID:30213934 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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