2MFS

Solution NMR structure of the cactus-derived antimicrobial peptide Ep-AMP1

2MFS の概要

• エントリーDOI: 10.2210/pdb2mfs/pdb
• NMR情報: BMRB: 19570
• 分子名称: Ep-AMP1 (1 entity in total)
• 機能のキーワード: cystine-knot, antimicrobial protein
• 由来する生物種: Synthetic
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3611.23

構造登録者

Rosengren, K.,Goransson, U.,Gunasekera, S.,Aboye, T.L. (登録日: 2013-10-22, 公開日: 2014-11-12, 最終更新日: 2024-11-06)

主引用文献

Aboye, T.L.,Stromstedt, A.A.,Gunasekera, S.,Bruhn, J.G.,El-Seedi, H.,Rosengren, K.J.,Goransson, U.
A cactus-derived toxin-like cystine knot Peptide with selective antimicrobial activity.
Chembiochem, 16:1068-1077, 2015

PubMed Abstract: Naturally occurring cystine knot peptides show a wide range of biological activity, and as they have inherent stability they represent potential scaffolds for peptide-based drug design and biomolecular engineering. Here we report the discovery, sequencing, chemical synthesis, three-dimensional solution structure determination and bioactivity of the first cystine knot peptide from Cactaceae (cactus) family: Ep-AMP1 from Echinopsis pachanoi. The structure of Ep-AMP1 (35 amino acids) conforms to that of the inhibitor cystine knot (or knottin) family but represents a novel diverse sequence; its activity was more than 500 times higher against bacterial than against eukaryotic cells. Rapid bactericidal action and liposome leakage implicate membrane permeabilisation as the mechanism of action. Sequence homology places Ec-AMP1 in the plant C6-type of antimicrobial peptides, but the three dimensional structure is highly similar to that of a spider neurotoxin.

PubMed: 25821084
DOI: 10.1002/cbic.201402704

実験手法

SOLUTION NMR