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2WGO

Structure of ranaspumin-2, a surfactant protein from the foam nests of a tropical frog

2WGO の概要
エントリーDOI10.2210/pdb2wgo/pdb
分子名称RANASPUMIN-2 (1 entity in total)
機能のキーワードcystatin fold, surfactant protein
由来する生物種ENGYSTOMOPS PUSTULOSUS (TUNGARA FROG)
タンパク質・核酸の鎖数1
化学式量合計11286.92
構造登録者
Mackenzie, C.D.,Smith, B.O.,Kennedy, M.W.,Cooper, A. (登録日: 2009-04-21, 公開日: 2009-06-23, 最終更新日: 2024-11-20)
主引用文献Mackenzie, C.D.,Smith, B.O.,Meister, A.,Blume, A.,Zhao, X.,Lu, J.R.,Kennedy, M.W.,Cooper, A.
Ranaspumin-2: Structure and Function of a Surfactant Protein from the Foam Nests of a Tropical Frog.
Biophys.J., 96:4984-, 2009
Cited by
PubMed Abstract: Ranaspumin-2 (Rsn-2) is a monomeric, 11 kDa surfactant protein identified as one of the major foam nest components of the túngara frog (Engystomops pustulosus), with an amino acid sequence unlike any other protein described so far. We report here on its structure in solution as determined by high-resolution NMR analysis, together with investigations of its conformation and packing at the air-water interface using a combination of infrared and neutron reflectivity techniques. Despite the lack of any significant sequence similarity, Rsn-2 in solution adopts a compact globular fold characteristic of the cystatin family, comprising a single helix over a four-stranded sheet, in a motif not previously associated with surfactant activity. The NMR structure of Rsn-2 shows no obvious amphiphilicity that might be anticipated for a surfactant protein. This suggests that it must undergo a significant conformational change when incorporated into the air-water interface that may involve a hinge-bending, clamshell opening of the separate helix and sheet segments to expose hydrophobic faces to air while maintaining the highly polar surfaces in contact with the underlying water layer. This model is supported by direct observation of the relative orientations of secondary structure elements at the interface by infrared reflection absorption spectroscopy, and by protein packing densities determined from neutron reflectivity profiles.
PubMed: 19527658
DOI: 10.1016/J.BPJ.2009.03.044
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 2wgo
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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