1aun: Difference between revisions
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'''PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM''' | '''PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM''' | ||
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[[Category: Sato, F.]] | [[Category: Sato, F.]] | ||
[[Category: Yamada, Y.]] | [[Category: Yamada, Y.]] | ||
[[Category: | [[Category: Antifungal protein]] | ||
[[Category: | [[Category: Osmotin]] | ||
[[Category: | [[Category: Pathogenesis-related protein]] | ||
[[Category: | [[Category: Pr-5d]] | ||
[[Category: | [[Category: Thaumatin-like protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:42:43 2008'' | |||
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Revision as of 07:42, 2 May 2008
PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM
Overview
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.
About this Structure
1AUN is a Single protein structure of sequence from Nicotiana tabacum. Full crystallographic information is available from OCA.
Reference
Crystal structure of tobacco PR-5d protein at 1.8 A resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins., Koiwa H, Kato H, Nakatsu T, Oda J, Yamada Y, Sato F, J Mol Biol. 1999 Mar 5;286(4):1137-45. PMID:10047487 Page seeded by OCA on Fri May 2 10:42:43 2008
