1aun Citations

Crystal structure of tobacco PR-5d protein at 1.8 A resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins.

J Mol Biol 286 1137-45 (1999)
Cited: 58 times
EuropePMC logo PMID: 10047487

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 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.

Articles - 1aun mentioned but not cited (8)

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Related citations provided by authors (1)

  1. Purification and characterization of tobacco pathogenesis-related protein PR-5d, an antifungal thaumatin-like protein.. Koiwa H, Kato H, Nakatsu T, Oda J, Yamada Y, Sato F Plant Cell Physiol 38 783-91 (1997)