1gh5 | pdb_00001gh5

ANTIFUNGAL PROTEIN FROM STREPTOMYCES TENDAE TU901, NMR AVERAGE STRUCTURE

spinqualitylabelsall models 1gh5, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1gh5 is a 1 chain structure with sequence from Streptomyces tendae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1g6e Gene: AFP (Streptomyces tendae) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed AFP1 is a recently discovered anti-fungal, chitin-binding protein from Streptomyces tendae Tu901. 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. Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces tendae TU901.,Campos-Olivas R, Horr I, Bormann C, Jung G, Gronenborn AM J Mol Biol. 2001 May 11;308(4):765-82. PMID:11350173 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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