6VE2

Tetradecameric PilQ bound by TsaP heptamer from Pseudomonas aeruginosa

6VE2 の概要

• エントリーDOI: 10.2210/pdb6ve2/pdb
• EMDBエントリー: 21152 21153 21154
• 分子名称: Fimbrial assembly protein PilQ, LysM domain-containing protein (2 entities in total)
• 機能のキーワード: type iv pilus, t4p, pilq, tsap, secretin, pilotin, type iva pilus, t4ap, pilus, outer membrane, periplasm, bacterial secretion system, protein transport
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1); 詳細
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 1379666.29

構造登録者

McCallum, M.,Tammam, S.,Rubinstein, J.L.,Burrows, L.L.,Howell, P.L. (登録日: 2019-12-28, 公開日: 2020-12-23, 最終更新日: 2024-03-06)

主引用文献

McCallum, M.,Tammam, S.,Rubinstein, J.L.,Burrows, L.L.,Howell, P.L.
CryoEM map of Pseudomonas aeruginosa PilQ enables structural characterization of TsaP.
Structure, 29:457-, 2021

PubMed Abstract: The type IV pilus machinery is a multi-protein complex that polymerizes and depolymerizes a pilus fiber used for attachment, twitching motility, phage adsorption, natural competence, protein secretion, and surface-sensing. An outer membrane secretin pore is required for passage of the pilus fiber out of the cell. Herein, the structure of the tetradecameric secretin, PilQ, from the Pseudomonas aeruginosa type IVa pilus system was determined to 4.3 Å and 4.4 Å resolution in the presence and absence of C symmetric spikes, respectively. The heptameric spikes were found to be two tandem C-terminal domains of TsaP. TsaP forms a belt around PilQ and while it is not essential for twitching motility, overexpression of TsaP triggers a signal cascade upstream of PilY1 leading to cyclic di-GMP up-regulation. These results resolve the identity of the spikes identified with Proteobacterial PilQ homologs and may reveal a new component of the surface-sensing cyclic di-GMP signal cascade.

PubMed: 33338410
DOI: 10.1016/j.str.2020.11.019

実験手法

ELECTRON MICROSCOPY (4.3 Å)