1I2V

NMR SOLUTION STRUCTURES OF AN ANTIFUNGAL AND ANTIBACTERIAL MUTANT OF HELIOMICIN

1I2V の概要

• エントリーDOI: 10.2210/pdb1i2v/pdb
• 関連するPDBエントリー: 1I2U
• NMR情報: BMRB: 5033
• 分子名称: DEFENSIN HELIOMICIN (1 entity in total)
• 機能のキーワード: alpha-beta protein, csab motif (cysteine stabilized alpha-helix beta-sheet motif), antimicrobial protein
• 由来する生物種: Heliothis virescens (tobacco budworm)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4736.31

構造登録者

Lamberty, M.,Caille, A.,Landon, C.,Tassin-Moindrot, S.,Hetru, C.,Bulet, P.,Vovelle, F. (登録日: 2001-02-12, 公開日: 2002-02-12, 最終更新日: 2024-11-20)

主引用文献

Lamberty, M.,Caille, A.,Landon, C.,Tassin-Moindrot, S.,Hetru, C.,Bulet, P.,Vovelle, F.
Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities.
Biochemistry, 40:11995-12003, 2001

PubMed Abstract: In response to an experimental infection, the lepidopteran Heliothis virescens produces an antifungal protein named heliomicin. Heliomicin displays sequence similarities with antifungal plant defensins and antibacterial or antifungal insect defensins. To gain information about the structural elements required for either antifungal or antibacterial activity, heliomicin and selected point-mutated variants were expressed in yeast as fusion proteins. The effects of mutations, defined by comparing the primary structure of heliomicin with the sequences of members of the insect defensin family, were analyzed using antibacterial and antifungal assays. One of the variants shows significant activity against Gram-positive bacteria while remaining efficient against fungi. The three-dimensional structures of this variant and of the wild-type protein were determined by two-dimensional (1)H NMR to establish a correlation between structure and antibacterial or antifungal activity. Wild-type and mutated heliomicins adopt a similar scaffold, including the so-called cysteine-stabilized alphabeta motif. A comparison of their structures with other defensin-type molecules indicates that common hydrophobic characteristics can be assigned to all the antifungal proteins. A comparative analysis of various structural features of heliomicin mutant and of antibacterial defensins enables common properties to be assessed, which will help to design new mutants with increased antibacterial activity.

PubMed: 11580275
DOI: 10.1021/bi0103563

実験手法

SOLUTION NMR