Crystal structure of tobacco PR-5d protein at 1.8 A resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins.
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.
Faculty of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
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Koiwa
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Kato
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Nakatsu
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Oda
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Yamada
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Sato
D000595:Amino Acid Sequence; D000935:Antifungal Agents / Q000737:chemistry; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D010947:Plants, Toxic; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013549:Sweetening Agents; D014026:Nicotiana / Q000737:chemistry*
D000935:Antifungal Agents; D010940:Plant Proteins; D013549:Sweetening Agents; C053376:pathogenesis-related proteins, plant; C003427:thaumatin protein, plant