| pubmed-article:10047487 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10047487 | lifeskim:mentions | umls-concept:C0003308 | lld:lifeskim |
| pubmed-article:10047487 | lifeskim:mentions | umls-concept:C0040329 | lld:lifeskim |
| pubmed-article:10047487 | lifeskim:mentions | umls-concept:C0205242 | lld:lifeskim |
| pubmed-article:10047487 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10047487 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:10047487 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:10047487 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10047487 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:10047487 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10047487 | pubmed:dateCreated | 1999-4-15 | lld:pubmed |
| pubmed-article:10047487 | pubmed:abstractText | 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. | lld:pubmed |
| pubmed-article:10047487 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10047487 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10047487 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10047487 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10047487 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10047487 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10047487 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10047487 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:10047487 | pubmed:author | pubmed-author:YamadaYY | lld:pubmed |
| pubmed-article:10047487 | pubmed:author | pubmed-author:KatzEE | lld:pubmed |
| pubmed-article:10047487 | pubmed:author | pubmed-author:SatoFF | lld:pubmed |
| pubmed-article:10047487 | pubmed:author | pubmed-author:OdaJJ | lld:pubmed |
| pubmed-article:10047487 | pubmed:author | pubmed-author:NakatsuTT | lld:pubmed |
| pubmed-article:10047487 | pubmed:author | pubmed-author:KoiwaHH | lld:pubmed |
| pubmed-article:10047487 | pubmed:copyrightInfo | Copyright 1999 Academic Press. | lld:pubmed |
| pubmed-article:10047487 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10047487 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:10047487 | pubmed:volume | 286 | lld:pubmed |
| pubmed-article:10047487 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10047487 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10047487 | pubmed:pagination | 1137-45 | lld:pubmed |
| pubmed-article:10047487 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10047487 | pubmed:meshHeading | pubmed-meshheading:10047487... | lld:pubmed |
| pubmed-article:10047487 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10047487 | pubmed:articleTitle | Crystal structure of tobacco PR-5d protein at 1.8 A resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins. | lld:pubmed |
| pubmed-article:10047487 | pubmed:affiliation | Faculty of Agriculture, Kyoto University, Kyoto 606-8502, Japan. | lld:pubmed |
| pubmed-article:10047487 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10047487 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:10047487 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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