4LSI

Ion selectivity of OmpF porin soaked in 0.3M KBr

4LSI の概要

• エントリーDOI: 10.2210/pdb4lsi/pdb
• 関連するPDBエントリー: 4LSE 4LSF 4LSH
• 分子名称: Outer membrane protein F, DI(HYDROXYETHYL)ETHER, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (7 entities in total)
• 機能のキーワード: porin, outer membrane protein, beta-barrel, ion transport, transport protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P02931
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 114976.69

構造登録者

Balasundaresan, D.,Blachowicz, L.,Roux, B. (登録日: 2013-07-22, 公開日: 2013-10-23, 最終更新日: 2023-09-20)

主引用文献

Dhakshnamoorthy, B.,Ziervogel, B.K.,Blachowicz, L.,Roux, B.
A structural study of ion permeation in OmpF porin from anomalous X-ray diffraction and molecular dynamics simulations.
J.Am.Chem.Soc., 135:16561-16568, 2013

PubMed Abstract: OmpF, a multiionic porin from Escherichia coli, is a useful protypical model system for addressing general questions about electrostatic interactions in the confinement of an aqueous molecular pore. Here, favorable anion locations in the OmpF pore were mapped by anomalous X-ray scattering of Br(–) ions from four different crystal structures and compared with Mg(2+) sites and Rb(+) sites from a previous anomalous diffraction study to provide a complete picture of cation and anion transfer paths along the OmpF channel. By comparing structures with various crystallization conditions, we find that anions bind in discrete clusters along the entire length of the OmpF pore, whereas cations find conserved binding sites with the extracellular, surface-exposed loops. Results from molecular dynamics simulations are consistent with the experimental data and help highlight the critical residues that preferentially contact either cations or anions during permeation. Analysis of these results provides new insights into the molecular mechanisms that determine ion selectivity in OmpF porin.

PubMed: 24106986
DOI: 10.1021/ja407783a

実験手法

X-RAY DIFFRACTION (2.089 Å)