2N6P

Solution NMR structure of Outer Membrane Protein G P92A mutant from Pseudomonas aeruginosa

2N6P の概要

• エントリーDOI: 10.2210/pdb2n6p/pdb
• 関連するPDBエントリー: 2n6l
• NMR情報: BMRB: 25776
• 分子名称: Outer membrane protein OprG (1 entity in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23688.60

構造登録者

Kucharska, I.,Seelheim, P.,Edrington, T.C.,Liang, B.,Tamm, L.K. (登録日: 2015-08-27, 公開日: 2015-12-30, 最終更新日: 2024-05-15)

主引用文献

Kucharska, I.,Seelheim, P.,Edrington, T.,Liang, B.,Tamm, L.K.
OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa.
Structure, 23:2234-2245, 2015

PubMed Abstract: OprG is an outer membrane protein of Pseudomonas aeruginosa whose function as an antibiotic-sensitive porin has been controversial and not well defined. Circumstantial evidence led to the proposal that OprG might transport hydrophobic compounds by using a lateral gate in the barrel wall thought to be lined by three conserved prolines. To test this hypothesis and to find the physiological substrates of OprG, we reconstituted the purified protein into liposomes and found it to facilitate the transport of small amino acids such as glycine, alanine, valine, and serine, which was confirmed by Pseudomonas growth assays. The structures of wild-type and a critical proline mutant were determined by nuclear magnetic resonance in dihexanoyl-phosphatidylcholine micellar solutions. Both proteins formed eight-stranded β-barrels with flexible extracellular loops. The interfacial prolines did not form a lateral gate in these structures, but loop 3 exhibited restricted motions in the inactive P92A mutant but not in wild-type OprG.

PubMed: 26655471
DOI: 10.1016/j.str.2015.10.009

実験手法

SOLUTION NMR