1GH5

ANTIFUNGAL PROTEIN FROM STREPTOMYCES TENDAE TU901, NMR AVERAGE STRUCTURE

1GH5 の概要

• エントリーDOI: 10.2210/pdb1gh5/pdb
• 関連するPDBエントリー: 1g6e
• 分子名称: ANTIFUNGAL PROTEIN (1 entity in total)
• 機能のキーワード: all-beta, two antiparallel beta-sheets, parallel beta-sandwich, antifungal protein
• 由来する生物種: Streptomyces tendae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10000.16

構造登録者

Campos-Olivas, R.,Bormann, C.,Hoerr, I.,Jung, G.,Gronenborn, A.M. (登録日: 2000-11-04, 公開日: 2001-03-28, 最終更新日: 2024-10-30)

主引用文献

Campos-Olivas, R.,Horr, I.,Bormann, C.,Jung, G.,Gronenborn, A.M.
Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces tendae TU901.
J.Mol.Biol., 308:765-782, 2001

PubMed Abstract: AFP1 is a recently discovered anti-fungal, chitin-binding protein from Streptomyces tendae Tü901. Mature AFP1 comprises 86 residues and exhibits limited sequence similarity to the cellulose-binding domains of bacterial cellulases and xylanases. No similarity to the Cys and Gly-rich domains of plant chitin-binding proteins (e.g. agglutinins, lectins, hevein) is observed. AFP1 is the first chitin-binding protein from a bacterium for which anti-fungal activity was shown. Here, we report the three-dimensional solution structure of AFP1, determined by nuclear magnetic resonance spectroscopy. The protein contains two antiparallel beta-sheets (five and four beta-strands each), that pack against each other in a parallel beta-sandwich. This type of architecture is conserved in the functionally related family II of cellulose-binding domains, albeit with different connectivity. A similar fold is also observed in other unrelated proteins (spore coat protein from Myxococcus xanthus, beta-B2 and gamma-B crystallins from Bos taurus, canavalin from Jack bean). AFP1 is therefore classified as a new member of the betagamma-crystallin superfamily. The dynamics of the protein was characterized by NMR using amide 15N relaxation and solvent exchange data. We demonstrate that the protein exhibits an axially symmetric (oblate-like) rotational diffusion tensor whose principal axis coincides to within 15 degrees with that of the inertial tensor. After completion of the present structure of AFP1, an identical fold was reported for a Streptomyces killer toxin-like protein. Based on sequence comparisons and clustering of conserved residues on the protein surface for different cellulose and chitin-binding proteins, we postulate a putative sugar-binding site for AFP1. The inability of the protein to bind short chitin fragments suggests that certain particular architectural features of the solid chitin surface are crucial for the interaction.

PubMed: 11350173
DOI: 10.1006/jmbi.2001.4622

実験手法

SOLUTION NMR