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2L2R

Helical hairpin structure of a novel antimicrobial peptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli)

2L2R の概要
エントリーDOI10.2210/pdb2l2r/pdb
NMR情報BMRB: 17152
分子名称Antimicrobial peptide EcAMP1 (1 entity in total)
機能のキーワードdisulfide-stabilized helical hairpin, antifungal peptide, antimicrobial peptide, antimicrobial protein
由来する生物種Echinochloa crus-galli (cockspur grass, barnyard grass, Echinochloa crus-galli (L.) P. Beauv.)
タンパク質・核酸の鎖数1
化学式量合計4288.78
構造登録者
Nolde, S.B.,Barinov, N.A.,Balashova, T.A.,Arseniev, A.S.,Vassilevski, A.A.,Rogozhin, E.A.,Egorov, T.A.,Grishin, E.V. (登録日: 2010-08-26, 公開日: 2011-05-11, 最終更新日: 2024-10-09)
主引用文献Nolde, S.B.,Vassilevski, A.A.,Rogozhin, E.A.,Barinov, N.A.,Balashova, T.A.,Samsonova, O.V.,Baranov, Y.V.,Feofanov, A.V.,Egorov, T.A.,Arseniev, A.S.,Grishin, E.V.
Disulfide-stabilized Helical Hairpin Structure and Activity of a Novel Antifungal Peptide EcAMP1 from Seeds of Barnyard Grass (Echinochloa crus-galli).
J.Biol.Chem., 286:25145-25153, 2011
Cited by
PubMed Abstract: This study presents purification, activity characterization, and (1)H NMR study of the novel antifungal peptide EcAMP1 from kernels of barnyard grass Echinochloa crus-galli. The peptide adopts a disulfide-stabilized α-helical hairpin structure in aqueous solution and thus represents a novel fold among naturally occurring antimicrobial peptides. Micromolar concentrations of EcAMP1 were shown to inhibit growth of several fungal phytopathogens. Confocal microscopy revealed intensive EcAMP1 binding to the surface of fungal conidia followed by internalization and accumulation in the cytoplasm without disturbance of membrane integrity. Close spatial structure similarity between EcAMP1, the trypsin inhibitor VhTI from seeds of Veronica hederifolia, and some scorpion and cone snail toxins suggests natural elaboration of different functions on a common fold.
PubMed: 21561864
DOI: 10.1074/jbc.M110.200378
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2l2r
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件を2026-04-15に公開中

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