2N2L

NMR structure of yersinia pestis ail (attachment invasion locus) in decylphosphocholine micelles calculated with implicit membrane solvation

2N2L の概要

• エントリーDOI: 10.2210/pdb2n2l/pdb
• 関連するPDBエントリー: 2N2M
• 分子名称: Outer membrane protein X (1 entity in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Yersinia pestis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17492.40

構造登録者

Marassi, F.M.,Ding, Y.,Tian, Y.,Schwieters, C.D.,Yao, Y. (登録日: 2015-05-10, 公開日: 2015-07-22, 最終更新日: 2024-05-15)

主引用文献

Marassi, F.M.,Ding, Y.,Schwieters, C.D.,Tian, Y.,Yao, Y.
Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation.
J.Biomol.Nmr, 63:59-65, 2015

PubMed Abstract: The outer membrane protein Ail (attachment invasion locus) is a virulence factor of Yersinia pestis that mediates cell invasion, cell attachment and complement resistance. Here we describe its three-dimensional backbone structure determined in decyl-phosphocholine (DePC) micelles by NMR spectroscopy. The NMR structure was calculated using the membrane function of the implicit solvation potential, eefxPot, which we have developed to facilitate NMR structure calculations in a physically realistic environment. We show that the eefxPot force field guides the protein towards its native fold. The resulting structures provide information about the membrane-embedded global position of Ail, and have higher accuracy, higher precision and improved conformational properties, compared to the structures calculated with the standard repulsive potential.

PubMed: 26143069
DOI: 10.1007/s10858-015-9963-2

実験手法

SOLUTION NMR