7LKO

The PilB(N-terminal)-PilZ complex of the Type IV pilus from Xanthomonas citri (2.9 A)

7LKO の概要

• エントリーDOI: 10.2210/pdb7lko/pdb
• 分子名称: Pilus biogenesis protein, Type IV fimbriae assembly protein, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: type iv pilus, transport protein
• 由来する生物種: Xanthomonas axonopodis pv. citri; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 62851.55

構造登録者

Llontop, E.E.,Guzzo, C.R.,Farah, C.S. (登録日: 2021-02-02, 公開日: 2021-08-11, 最終更新日: 2024-04-03)

主引用文献

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

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: 34398935
DOI: 10.1371/journal.ppat.1009808

実験手法

X-RAY DIFFRACTION (2.88 Å)