2JNI

Spatial structure of antimicrobial peptide arenicin-2 in aqueous solution

2JNI の概要

• エントリーDOI: 10.2210/pdb2jni/pdb
• NMR情報: BMRB: 15115
• 分子名称: Arenicin-2 (1 entity in total)
• 機能のキーワード: antimicrobial, beta-sheet, antimicrobial protein
• 由来する生物種: Arenicola marina (lugworm)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2780.37

構造登録者

Ovchinnikova, T.V.,Shenkarev, Z.O.,Nadezhdin, K.D.,Balandin, S.V.,Zhmak, M.N.,Kudelina, I.A.,Finkina, E.I.,Kokryakov, V.N.,Arseniev, A.S. (登録日: 2007-01-25, 公開日: 2007-08-07, 最終更新日: 2023-12-20)

主引用文献

Ovchinnikova, T.V.,Shenkarev, Z.O.,Nadezhdin, K.D.,Balandin, S.V.,Zhmak, M.N.,Kudelina, I.A.,Finkina, E.I.,Kokryakov, V.N.,Arseniev, A.S.
Recombinant expression, synthesis, purification, and solution structure of arenicin
Biochem.Biophys.Res.Commun., 360:156-162, 2007

PubMed Abstract: Arenicins are 21-residue cationic antimicrobial peptides, isolated from marine polychaeta Arenicola marina. In order to determine a high-resolution three-dimensional structure of arenicin-2, the recombinant peptide was overexpressed as a fused form in Escherichia coli. Both arenicin isoforms were synthesized using the Fmoc-based solid-phase strategy. Recombinant and synthetic arenicins were purified, and their antimicrobial and spectroscopic properties were analyzed. NMR investigation shows that in water solution arenicin-2 displays a prolonged beta-hairpin, formed by two antiparallel beta-strands and stabilized by one disulfide and nine hydrogen bonds. A significant right-handed twist in the beta-sheet is deprived the peptide surface of amphipathicity. CD spectroscopic analysis indicates that arenicin-2 binds to the SDS and DPC micelles, and conformation of the peptide is significantly changed upon binding. Arenicin strongly binds to anionic lipid (POPE/POPG) vesicles in contrast with zwitterionic (POPC) ones. These results suggest that arenicins are membrane active peptides and point to possible mechanism of their selectivity toward bacterial cells.

PubMed: 17585874
DOI: 10.1016/j.bbrc.2007.06.029

実験手法

SOLUTION NMR