2LJ7

3D solution structure of plant defensin Lc-def

2LJ7 の概要

• エントリーDOI: 10.2210/pdb2lj7/pdb
• NMR情報: BMRB: 17923
• 分子名称: Defensin Lc-def (1 entity in total)
• 機能のキーワード: antimicrobial protein
• 由来する生物種: Lens culinaris subsp. culinaris (Cultivated lentil)
• 細胞内の位置: Secreted : B3F051
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5460.24

構造登録者

Shenkarev, Z.,Mineev, K.,Gizatullina, A. (登録日: 2011-09-07, 公開日: 2012-09-12, 最終更新日: 2024-11-20)

主引用文献

Shenkarev, Z.O.,Gizatullina, A.K.,Finkina, E.I.,Alekseeva, E.A.,Balandin, S.V.,Mineev, K.S.,Arseniev, A.S.,Ovchinnikova, T.V.
Heterologous expression and solution structure of defensin from lentil Lens culinaris.
Biochem.Biophys.Res.Commun., 451:252-257, 2014

PubMed Abstract: A new defensin Lc-def, isolated from germinated seeds of the lentil Lens culinaris, has molecular mass 5440.4Da and consists of 47 amino acid residues. Lc-def and its (15)N-labeled analog were overexpressed in Escherichia coli. Antimicrobial activity of the recombinant protein was examined, and its spatial structure, dynamics, and interaction with lipid vesicles were studied by NMR spectroscopy. It was shown that Lc-def is active against fungi, but does not inhibit the growth of Gram-positive and Gram-negative bacteria. The peptide is monomeric in aqueous solution and contains one α-helix and triple-stranded β-sheet, which form cysteine-stabilized αβ motif (CSαβ) previously found in other plant defensins. The sterically neighboring loop1 and loop3 protrude from the defensin core and demonstrate significant mobility on the μs-ms timescale. Lc-def does not bind to the zwitterionic lipid (POPC) vesicles but interacts with the partially anionic (POPC/DOPG, 7:3) membranes under low-salt conditions. The Lc-def antifungal activity might be mediated through electrostatic interaction with anionic lipid components of fungal membranes.

PubMed: 25086358
DOI: 10.1016/j.bbrc.2014.07.104

実験手法

SOLUTION NMR