1aun
From Proteopedia
(New page: 200px<br /><applet load="1aun" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aun, resolution 1.8Å" /> '''PATHOGENESIS-RELATED ...) |
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| - | [[Image:1aun.jpg|left|200px]]<br /><applet load="1aun" size=" | + | [[Image:1aun.jpg|left|200px]]<br /><applet load="1aun" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1aun, resolution 1.8Å" /> | caption="1aun, resolution 1.8Å" /> | ||
'''PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM'''<br /> | '''PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of tobacco PR-5d, an antifungal thaumatin-like | + | 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== | ==About this Structure== | ||
| - | 1AUN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http:// | + | 1AUN is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: thaumatin-like protein]] | [[Category: thaumatin-like protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:27 2008'' |
Revision as of 09:48, 21 February 2008
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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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