7w64

Crystal structure of minor pilin TcpB from Vibrio cholerae complexed with N-terminal peptide fragment of TcpF

spinqualitylabelsall models 7w64, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7w64 is a 12 chain structure with sequence from Vibrio cholerae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: 1PE, CA, CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TCPB_VIBCH Involved in TCP pilus biogenesis. Publication Abstract from PubMed Colonization of the host intestine is the most important step in Vibrio cholerae infection. The toxin-coregulated pilus (TCP), an operon-encoded type IVb pilus (T4bP), plays a crucial role in this process, which requires an additional secreted protein, TcpF, encoded on the same TCP operon; however, its mechanisms of secretion and function remain elusive. Here, we demonstrated that TcpF interacts with the minor pilin, TcpB, of TCP and elucidated the crystal structures of TcpB alone and in complex with TcpF. The structural analyses reveal how TCP recognizes TcpF and its secretory mechanism via TcpB-dependent pilus elongation and retraction. Upon binding to TCP, TcpF forms a flower-shaped homotrimer with its flexible N terminus hooked onto the trimeric interface of TcpB. Thus, the interaction between the minor pilin and the N terminus of the secreted protein, namely, the T4bP secretion signal, is key for V. cholerae colonization and is a new potential therapeutic target. Structural basis for the toxin-coregulated pilus-dependent secretion of Vibrio cholerae colonization factor.,Oki H, Kawahara K, Iimori M, Imoto Y, Nishiumi H, Maruno T, Uchiyama S, Muroga Y, Yoshida A, Yoshida T, Ohkubo T, Matsuda S, Iida T, Nakamura S Sci Adv. 2022 Oct 14;8(41):eabo3013. doi: 10.1126/sciadv.abo3013. Epub 2022 Oct , 14. PMID:36240278 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pilin 3D structures

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