8V7P

Crystal structure of the truncated P1 pilin from Pseudomonas aeruginosa

8V7P の概要

• エントリーDOI: 10.2210/pdb8v7p/pdb
• 分子名称: Fimbrial protein, CACODYLIC ACID (3 entities in total)
• 機能のキーワード: pilin protein, fimbrial protein, pseudomonas aeruginosa, cell adhesion
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13187.62

構造登録者

Bragagnolo, N.J.,Audette, G.F. (登録日: 2023-12-04, 公開日: 2024-12-11, 最終更新日: 2024-12-18)

主引用文献

Bragagnolo, N.,Audette, G.F.
The 1.3 angstrom resolution structure of the truncated group Ia type IV pilin from Pseudomonas aeruginosa strain P1.
Acta Crystallogr D Struct Biol, 80:834-849, 2024

PubMed Abstract: The type IV pilus is a diverse molecular machine capable of conferring a variety of functions and is produced by a wide range of bacterial species. The ability of the pilus to perform host-cell adherence makes it a viable target for the development of vaccines against infection by human pathogens such as Pseudomonas aeruginosa. Here, the 1.3 Å resolution crystal structure of the N-terminally truncated type IV pilin from P. aeruginosa strain P1 (ΔP1) is reported, the first structure of its phylogenetically linked group (group I) to be discussed in the literature. The structure was solved from X-ray diffraction data that were collected 20 years ago with a molecular-replacement search model generated using AlphaFold; the effectiveness of other search models was analyzed. Examination of the high-resolution ΔP1 structure revealed a solvent network that aids in maintaining the fold of the protein. On comparing the sequence and structure of P1 with a variety of type IV pilins, it was observed that there are cases of higher structural similarities between the phylogenetic groups of P. aeruginosa than there are between the same phylogenetic group, indicating that a structural grouping of pilins may be necessary in developing antivirulence drugs and vaccines. These analyses also identified the α-β loop as the most structurally diverse domain of the pilins, which could allow it to serve a role in pilus recognition. Studies of ΔP1 in vitro polymerization demonstrate that the optimal hydrophobic catalyst for the oligomerization of the pilus from strain K122 is not conducive for pilus formation of ΔP1; a model of a three-start helical assembly using the ΔP1 structure indicates that the α-β loop and the D-loop prevent in vitro polymerization.

PubMed: 39607821
DOI: 10.1107/S205979832401132X

実験手法

X-RAY DIFFRACTION (1.3 Å)