1aun: Difference between revisions

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[[Image:1aun.jpg|left|200px]]
{{Seed}}
[[Image:1aun.png|left|200px]]


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{{STRUCTURE_1aun|  PDB=1aun  |  SCENE=  }}  
{{STRUCTURE_1aun|  PDB=1aun  |  SCENE=  }}  


'''PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM'''
===PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM===




==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.
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:37:42 2008''

Revision as of 14:37, 30 June 2008

File:1aun.png

Template:STRUCTURE 1aun

PATHOGENESIS-RELATED PROTEIN 5D FROM NICOTIANA TABACUM

Template:ABSTRACT PUBMED 10047487

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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