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• W1991837864 abstract "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 Å. 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 Å and 1.542 °. 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 β-sheet in domain I. The acidic residues located in the hollow of the cleft form the β-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." @default.
• W1991837864 created "2016-06-24" @default.
• W1991837864 creator A5031484098 @default.
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• W1991837864 creator A5064027488 @default.
• W1991837864 date "1999-03-01" @default.
• W1991837864 modified "2023-10-09" @default.
• W1991837864 title "Crystal structure of tobacco PR-5d protein at 1.8 Å resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins" @default.
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• W1991837864 doi "https://doi.org/10.1006/jmbi.1998.2540" @default.
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