- EMDB-21153: Tetradecameric PilQ from Pseudomonas aeruginosa -
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基本情報
登録情報
データベース: EMDB / ID: EMD-21153
タイトル
Tetradecameric PilQ from Pseudomonas aeruginosa
マップデータ
Sharpened z-flipped map
試料
複合体: Tetradecameric PilQ from Pseudomonas aeruginosa
タンパク質・ペプチド: Fimbrial assembly protein PilQ
キーワード
Type IV pilus / T4P / PilQ / secretin / type IVa pilus / T4aP / pilus / outer membrane / periplasm / bacterial secretion system / PROTEIN TRANSPORT
機能・相同性
機能・相同性情報
type IV pilus assembly / protein secretion / cell outer membrane 類似検索 - 分子機能
: / Type IV pilus secretin PilQ / AMIN domain / AMIN domain / Secretin and TonB N terminus short domain / Secretin/TonB, short N-terminal domain / Secretin and TonB N terminus short domain / GspD/PilQ family / Bacterial type II secretion system protein D signature. / Type II secretion system protein GspD, conserved site ...: / Type IV pilus secretin PilQ / AMIN domain / AMIN domain / Secretin and TonB N terminus short domain / Secretin/TonB, short N-terminal domain / Secretin and TonB N terminus short domain / GspD/PilQ family / Bacterial type II secretion system protein D signature. / Type II secretion system protein GspD, conserved site / NolW-like / Bacterial type II/III secretion system short domain / NolW-like superfamily / Type II/III secretion system / Bacterial type II and III secretion system protein 類似検索 - ドメイン・相同性
ジャーナル: Structure / 年: 2021 タイトル: CryoEM map of Pseudomonas aeruginosa PilQ enables structural characterization of TsaP. 著者: Matthew McCallum / Stephanie Tammam / John L Rubinstein / Lori L Burrows / P Lynne Howell / 要旨: 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 ...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.