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

被引:110
作者
Koiwa, H
Kato, H
Nakatsu, T
Oda, J
Yamada, Y
Sato, F [1 ]
机构
[1] Kyoto Univ, Fac Agr, Grad Sch, Div Appl Life Sci, Kyoto 6068502, Japan
[2] Kyoto Univ, Inst Chem Res, Uji, Kyoto 6110011, Japan
[3] Nara Adv Inst Sci & Technol, Grad Sch Biol Sci, Nara 6300101, Japan
基金
日本学术振兴会;
关键词
antifungal activity; osmotin; pathogenesis-related protein; tobacco; zeamatin;
D O I
10.1006/jmbi.1998.2540
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom. The structure consists of 208 amino acid residues and 89 water 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. 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. (C) 1999 Academic Press.
引用
收藏
页码:1137 / 1145
页数:9
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