4D64

Structure of porin Omp-Pst1 from P. stuartii; the crystallographic symmetry generates a dimer of trimers.

4D64 の概要

• エントリーDOI: 10.2210/pdb4d64/pdb
• 関連するPDBエントリー: 4D5W 4D5X 4D65
• 分子名称: PORIN 1, CALCIUM ION (3 entities in total)
• 機能のキーワード: transport protein, bacterial junction, steric-zipper, dimer of trimers
• 由来する生物種: PROVIDENCIA STUARTII
• 細胞内の位置: Cell outer membrane ; Multi-pass membrane protein : E3U904
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 117143.66

構造登録者

Nasrallah, C.,Colletier, J.P. (登録日: 2014-11-08, 公開日: 2016-03-09, 最終更新日: 2023-12-20)

主引用文献

El-Khatib, M.,Nasrallah, C.,Lopes, J.,Tran, Q.T.,Tetreau, G.,Basbous, H.,Fenel, D.,Gallet, B.,Lethier, M.,Bolla, J.M.,Pages, J.M.,Vivaudou, M.,Weik, M.,Winterhalter, M.,Colletier, J.P.
Porin self-association enables cell-to-cell contact inProvidencia stuartiifloating communities.
Proc. Natl. Acad. Sci. U.S.A., 115:E2220-E2228, 2018

PubMed Abstract: The gram-negative pathogen forms floating communities within which adjacent cells are in apparent contact, before depositing as canonical surface-attached biofilms. Because porins are the most abundant proteins in the outer membrane of gram-negative bacteria, we hypothesized that they could be involved in cell-to-cell contact and undertook a structure-function relationship study on the two porins of , Omp-Pst1 and Omp-Pst2. Our crystal structures reveal that these porins can self-associate through their extracellular loops, forming dimers of trimers (DOTs) that could enable cell-to-cell contact within floating communities. Support for this hypothesis was obtained by studying the porin-dependent aggregation of liposomes and model cells. The observation that facing channels are open in the two porin structures suggests that DOTs could not only promote cell-to-cell contact but also contribute to intercellular communication.

PubMed: 29476011
DOI: 10.1073/pnas.1714582115

実験手法

X-RAY DIFFRACTION (3.2 Å)