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spinqualitylabelsall models 1aun, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM

Overview

The crystal structure of tobacco PR-5d, an antifungal thaumatin-like, protein isolated from cultured tobacco cells, was determined at the, resolution of 1.8 A. The structure consists of 208 amino acid residues and, 89 water molecules with a crystallographic R-factor of 0.169. The model, has good stereochemistry, with respective root-mean-square deviations from, the ideal values for bond and angle distances of 0.007 A and 1.542, degrees. Of the homologous PR-5 proteins, only those with antifungal, activity had a common motif, a negatively charged surface cleft. This, cleft is at the boundary between domains I and II, with a bottom part, consisting of a three-stranded antiparallel beta-sheet in domain I. The, acidic residues located in the hollow of the cleft form the beta-sheet, region. Sequence and secondary structure analyses showed that the amino, acid residues comprising the acidic cleft of PR-5d are conserved among, other antifungal PR-5 proteins. This is the first report on the, high-resolution crystal structure of an antifungal PR-5 protein. This, structure provides insight into the function of pathogenesis-related, proteins.

About this Structure

1AUN is a Single protein structure of sequence from Nicotiana tabacum. Full crystallographic information is available from OCA.

Reference

Crystal structure of tobacco PR-5d protein at 1.8 A resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins., Koiwa H, Kato H, Nakatsu T, Oda J, Yamada Y, Sato F, J Mol Biol. 1999 Mar 5;286(4):1137-45. PMID:10047487

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