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

The crystal structure of tobacco PR-5d, an antifungal thaumatin-like protei n isolated from cultured tobacco cells, was determined at the resolution of 1.8 Angstrom. The structure consists of 208 amino acid residues and 89 wat er molecules with a crystallographic X-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 Angstrom and 1.542 degrees. O f the homologous PR-5 proteins, only those with antifungal activity had a c ommon motif, a negatively charged surface cleft. This cleft is at the bound ary between domains I and II, with a bottom part consisting of a three-stra nded antiparallel beta-sheet in domain I. The acidic residues located in th e hollow of the cleft form the beta-sheet region. Sequence and secondary st ructure 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 pathogen esis-related proteins. (C) 1999 Academic Press.