1AUN
PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM
Summary for 1AUN
| Entry DOI | 10.2210/pdb1aun/pdb |
| Descriptor | PR-5D (2 entities in total) |
| Functional Keywords | antifungal protein, pathogenesis-related protein, pr-5d, osmotin, thaumatin-like protein |
| Biological source | Nicotiana tabacum (common tobacco) |
| Total number of polymer chains | 1 |
| Total formula weight | 22778.50 |
| Authors | Koiwa, H.,Kato, H.,Nakatsu, T.,Oda, J.,Yamada, Y.,Sato, F. (deposition date: 1997-08-29, release date: 1998-03-04, Last modification date: 2024-10-16) |
| Primary citation | Koiwa, H.,Kato, H.,Nakatsu, T.,Oda, J.,Yamada, Y.,Sato, F. 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., 286:1137-1145, 1999 Cited by PubMed 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. PubMed: 10047487DOI: 10.1006/jmbi.1998.2540 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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