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| {{STRUCTURE_1aun| PDB=1aun | SCENE= }} | | {{STRUCTURE_1aun| PDB=1aun | SCENE= }} |
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| '''PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM'''
| | ===PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_10047487}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10047487 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10047487}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Pr-5d]] | | [[Category: Pr-5d]] |
| [[Category: Thaumatin-like protein]] | | [[Category: Thaumatin-like protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:42:43 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:37:42 2008'' |
