1aun: Difference between revisions
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[[Image:1aun.jpg|left|200px]] | [[Image:1aun.jpg|left|200px]] | ||
'''PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM''' | {{Structure | ||
|PDB= 1aun |SIZE=350|CAPTION= <scene name='initialview01'>1aun</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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}} | |||
'''PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AUN is a [ | 1AUN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUN OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10047487 10047487] | ||
[[Category: Nicotiana tabacum]] | [[Category: Nicotiana tabacum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thaumatin-like protein]] | [[Category: thaumatin-like protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:27 2008'' | ||
Revision as of 08:02, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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