5OWF

Structure of a LAO-binding protein mutant with glutamine

5OWF の概要

• エントリーDOI: 10.2210/pdb5owf/pdb
• 分子名称: Lysine/arginine/ornithine-binding periplasmic protein, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (6 entities in total)
• 機能のキーワード: ligand specificity, protein design, binding pocket, periplasmatic binding protein, transport protein
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Periplasm : P02911
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29930.57

構造登録者

Shanmugaratnam, S.,Banda-Vazquez, J.,Sosa-Peinado, A.,Hocker, B. (登録日: 2017-08-31, 公開日: 2018-03-21, 最終更新日: 2024-11-06)

主引用文献

Banda-Vazquez, J.,Shanmugaratnam, S.,Rodriguez-Sotres, R.,Torres-Larios, A.,Hocker, B.,Sosa-Peinado, A.
Redesign of LAOBP to bind novel l-amino acid ligands.
Protein Sci., 27:957-968, 2018

PubMed Abstract: Computational protein design is still a challenge for advancing structure-function relationships. While recent advances in this field are promising, more information for genuine predictions is needed. Here, we discuss different approaches applied to install novel glutamine (Gln) binding into the Lysine/Arginine/Ornithine binding protein (LAOBP) from Salmonella typhimurium. We studied the ligand binding behavior of two mutants: a binding pocket grafting design based on a structural superposition of LAOBP to the Gln binding protein QBP from Escherichia coli and a design based on statistical coupled positions. The latter showed the ability to bind Gln even though the protein was not very stable. Comparison of both approaches highlighted a nonconservative shared point mutation between LAOBP_graft and LAOBP_sca. This context dependent L117K mutation in LAOBP turned out to be sufficient for introducing Gln binding, as confirmed by different experimental techniques. Moreover, the crystal structure of LAOBP_L117K in complex with its ligand is reported.

PubMed: 29524280
DOI: 10.1002/pro.3403

実験手法

X-RAY DIFFRACTION (1.91 Å)