2M8B

Solution structure of AhPDF1 from Arabidopsis halleri

2M8B の概要

• エントリーDOI: 10.2210/pdb2m8b/pdb
• NMR情報: BMRB: 19237
• 分子名称: plant defensin PDF1.1 (1 entity in total)
• 機能のキーワード: csab, 4 disulfide bridges, plant defensin, plant protein
• 由来する生物種: Arabidopsis halleri
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5699.60

構造登録者

Meindre, F.,Paquet, F.,Landon, C. (登録日: 2013-05-13, 公開日: 2014-05-14, 最終更新日: 2024-11-20)

主引用文献

Meindre, F.,Lelievre, D.,Loth, K.,Mith, O.,Aucagne, V.,Berthomieu, P.,Marques, L.,Delmas, A.F.,Landon, C.,Paquet, F.
The nuclear magnetic resonance solution structure of the synthetic AhPDF1.1b plant defensin evidences the structural feature within the gamma-motif.
Biochemistry, 53:7745-7754, 2014

PubMed Abstract: Plant defensins (PDF) are cysteine-rich peptides that are major actors in the innate immunity in plants. Besides their antifungal activity, some PDF such as Arabidopsis halleri PDF1.1b confer zinc tolerance in plants. Here we present (i) an efficient protocol for the production of AhPDF1.1b by solid-phase peptide synthesis followed by controlled oxidative folding to obtain the highly pure native form of the defensin and (ii) the three-dimensional (3D) nuclear magnetic resonance structure of AhPDF1.1b, the first 3D structure of plant defensin obtained with a synthetic peptide. Its fold is organized around the typical cysteine-stabilized α-helix β-sheet motif and contains the γ-core motif involved in the antifungal activity of all plant defensins. On the basis of our structural analysis of AhPDF1 defensins combined with previous biological data for antifungal and zinc tolerance activities, we established the essential role of cis-Pro41 within the γ-core. In fact, the four consecutive residues (Val39-Phe40-Pro41-Ala42) are strictly conserved for plant defensins able to tolerate zinc. We hypothesized that structural and/or dynamic features of this sequence are related to the ability of the defensin to chelate zinc.

PubMed: 25419866
DOI: 10.1021/bi501285k

実験手法

SOLUTION NMR