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8Q2C

Crystal structure of the E. coli PqiC Lipoprotein

8Q2C の概要
エントリーDOI10.2210/pdb8q2c/pdb
分子名称Intermembrane transport lipoprotein PqiC (1 entity in total)
機能のキーワードoutermembrane lipoprotein, transport protein
由来する生物種Escherichia coli
タンパク質・核酸の鎖数2
化学式量合計43440.88
構造登録者
Cooper, B.F.,Ratkeviciute, G.R.,Knowles, T.J. (登録日: 2023-08-02, 公開日: 2023-09-20, 最終更新日: 2024-01-31)
主引用文献Cooper, B.F.,Ratkeviciute, G.,Clifton, L.A.,Johnston, H.,Holyfield, R.,Hardy, D.J.,Caulton, S.G.,Chatterton, W.,Sridhar, P.,Wotherspoon, P.,Hughes, G.W.,Hall, S.C.,Lovering, A.L.,Knowles, T.J.
An octameric PqiC toroid stabilises the outer-membrane interaction of the PqiABC transport system.
Embo Rep., 25:82-101, 2024
Cited by
PubMed Abstract: The E. coli Paraquat Inducible (Pqi) Pathway is a putative Gram-negative phospholipid transport system. The pathway comprises three components: an integral inner membrane protein (PqiA), a periplasmic spanning MCE family protein (PqiB) and an outer membrane lipoprotein (PqiC). Interactions between all complex components, including stoichiometry, remain uncharacterised; nevertheless, once assembled into their quaternary complex, the trio of Pqi proteins are anticipated to provide a continuous channel between the inner and outer membranes of diderms. Here, we present X-ray structures of both the native and a truncated, soluble construct of the PqiC lipoprotein, providing insight into its biological assembly, and utilise neutron reflectometry to characterise the nature of the PqiB-PqiC-membrane interaction. Finally, we employ phenotypic complementation assays to probe specific PqiC residues, which imply the interaction between PqiB and PqiC is less intimate than previously anticipated.
PubMed: 38228789
DOI: 10.1038/s44319-023-00014-4
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.21 Å)
構造検証レポート
Validation report summary of 8q2c
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-18に公開中

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