2N2Z

NMR spatial structure of nonspecific lipid transfer protein from the dill Anethum graveolens L.

2N2Z の概要

• エントリーDOI: 10.2210/pdb2n2z/pdb
• NMR情報: BMRB: 25630
• 分子名称: Non-specific lipid-transfer protein (1 entity in total)
• 機能のキーワード: lipid transfer protein, plant defense protein, plant protein
• 由来する生物種: Anethum graveolens (dill)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9541.06

構造登録者

Mineev, K.S.,Melnikova, D.N.,Finkina, E.I.,Arseniev, A.S.,Ovchinnikova, T.V. (登録日: 2015-05-19, 公開日: 2016-03-30, 最終更新日: 2024-10-09)

主引用文献

Melnikova, D.N.,Mineev, K.S.,Finkina, E.I.,Arseniev, A.S.,Ovchinnikova, T.V.
A novel lipid transfer protein from the dill Anethum graveolens L.: isolation, structure, heterologous expression, and functional characteristics.
J.Pept.Sci., 22:59-66, 2016

PubMed Abstract: A novel lipid transfer protein, designated as Ag-LTP, was isolated from aerial parts of the dill Anethum graveolens L. Structural, antimicrobial, and lipid binding properties of the protein were studied. Complete amino acid sequence of Ag-LTP was determined. The protein has molecular mass of 9524.4 Da, consists of 93 amino acid residues including eight cysteines forming four disulfide bonds. The recombinant Ag-LTP was overexpressed in Escherichia coli and purified. NMR investigation shows that the Ag-LTP spatial structure contains four α-helices, forming the internal hydrophobic cavity, and a long C-terminal tail. The measured volume of the Ag-LTP hydrophobic cavity is equal to ~800 A(3), which is much larger than those of other plant LTP1s. Ag-LTP has weak antifungal activity and unpronounced lipid binding specificity but effectively binds plant hormone jasmonic acid. Our results afford further molecular insight into biological functions of LTP in plants.

PubMed: 26680443
DOI: 10.1002/psc.2840

実験手法

SOLUTION NMR