4QL0

Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)

4QL0 の概要

• エントリーDOI: 10.2210/pdb4ql0/pdb
• 関連するPDBエントリー: 2QDZ 4QKY
• 分子名称: Filamentous hemagglutinin transporter protein FhaC, TRIETHYLENE GLYCOL, DI(HYDROXYETHYL)ETHER, ... (9 entities in total)
• 機能のキーワード: beta-barrel, potra domain, protein transport, outer membrane
• 由来する生物種: Bordetella pertussis
• 細胞内の位置: Cell outer membrane : P35077
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 63358.96

構造登録者

Maier, T.,Clantin, B.,Gruss, F.,Dewitte, F.,Delattre, A.S.,Jacob-Dubuisson, F.,Hiller, S.,Villeret, V. (登録日: 2014-06-10, 公開日: 2015-06-17, 最終更新日: 2023-11-08)

主引用文献

Maier, T.,Clantin, B.,Gruss, F.,Dewitte, F.,Delattre, A.S.,Jacob-Dubuisson, F.,Hiller, S.,Villeret, V.
Conserved Omp85 lid-lock structure and substrate recognition in FhaC
Nat Commun, 6:7452-7452, 2015

PubMed Abstract: Omp85 proteins mediate translocation of polypeptide substrates across and into cellular membranes. They share a common architecture comprising substrate-interacting POTRA domains, a C-terminal 16-stranded β-barrel pore and two signature motifs located on the inner barrel wall and at the tip of the extended L6 loop. The observation of two distinct conformations of the L6 loop in the available Omp85 structures previously suggested a functional role of conformational changes in L6 in the Omp85 mechanism. Here we present a 2.5 Å resolution structure of a variant of the Omp85 secretion protein FhaC, in which the two signature motifs interact tightly and form the conserved 'lid lock'. Reanalysis of previous structural data shows that L6 adopts the same, conserved resting state position in all available Omp85 structures. The FhaC variant structure further reveals a competitive mechanism for the regulation of substrate binding mediated by the linker to the N-terminal plug helix H1.

PubMed: 26058369
DOI: 10.1038/ncomms8452

実験手法

X-RAY DIFFRACTION (2.5 Å)