7LKN
The PilB(N-terminal_P70S mutant)-PilZ complex (SeMet)
Summary for 7LKN
| Entry DOI | 10.2210/pdb7lkn/pdb |
| Descriptor | Pilus biogenesis protein, Type IV fimbriae assembly protein, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | type iv pilus, transport protein |
| Biological source | Xanthomonas axonopodis pv. citri More |
| Total number of polymer chains | 4 |
| Total formula weight | 63963.78 |
| Authors | Llontop, E.E.,Guzzo, C.R.,Farah, C.S. (deposition date: 2021-02-02, release date: 2021-08-11, Last modification date: 2024-10-30) |
| Primary citation | Llontop, E.E.,Cenens, W.,Favaro, D.C.,Sgro, G.G.,Salinas, R.K.,Guzzo, C.R.,Farah, C.S. The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri. Plos Pathog., 17:e1009808-e1009808, 2021 Cited by PubMed Abstract: Type IV pili (T4P) are thin and flexible filaments found on the surface of a wide range of Gram-negative bacteria that undergo cycles of extension and retraction and participate in a variety of important functions related to lifestyle, defense and pathogenesis. During pilus extensions, the PilB ATPase energizes the polymerization of pilin monomers from the inner membrane. In Xanthomonas citri, two cytosolic proteins, PilZ and the c-di-GMP receptor FimX, are involved in the regulation of T4P biogenesis through interactions with PilB. In vivo fluorescence microscopy studies show that PilB, PilZ and FimX all colocalize to the leading poles of X. citri cells during twitching motility and that this colocalization is dependent on the presence of all three proteins. We demonstrate that full-length PilB, PilZ and FimX can interact to form a stable complex as can PilB N-terminal, PilZ and FimX C-terminal fragments. We present the crystal structures of two binary complexes: i) that of the PilB N-terminal domain, encompassing sub-domains ND0 and ND1, bound to PilZ and ii) PilZ bound to the FimX EAL domain within a larger fragment containing both GGDEF and EAL domains. Evaluation of PilZ interactions with PilB and the FimX EAL domain in these and previously published structures, in conjunction with mutagenesis studies and functional assays, allow us to propose an internally consistent model for the PilB-PilZ-FimX complex and its interactions with the PilM-PilN complex in the context of the inner membrane platform of the X. citri Type IV pilus. PubMed: 34398935DOI: 10.1371/journal.ppat.1009808 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.71 Å) |
Structure validation
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