Source:http://linkedlifedata.com/resource/pubmed/id/18406424
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2008-4-29
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pubmed:databankReference | |
pubmed:abstractText |
Plant pathogenesis-related (PR) proteins of class 10 (PR-10) are small and cytosolic. The main feature of their three-dimensional structure is a large cavity between a seven-stranded antiparallel beta-sheet and a long C-terminal alpha-helix. Although PR-10 proteins are abundant in plants, their physiological role remains unknown. Recent data have indicated ligand binding as their possible biological function. The article describes the structure of a complex between a classic PR-10 protein (yellow lupine LlPR-10.2B) and the plant hormone, trans-zeatin. Previously, trans-zeatin binding has been reported in a structurally related cytokinin-specific binding protein, which has a distant sequence relation with classic PR-10 proteins. In the present 1.35 A resolution crystallographic model, three perfectly ordered zeatin molecules are found in the binding cavity of the protein. The fact that three zeatin molecules are bound by the protein when only a fourfold molar excess of the ligand was used indicates an unusual type of affinity for this ligand and suggests that LlPR-10.2B, and perhaps other PR-10 proteins as well, acts as a reservoir of cytokinin molecules in the aqueous environment of the cell.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytokinins,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Growth Regulators,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Zeatin,
http://linkedlifedata.com/resource/pubmed/chemical/pathogenesis-related proteins, plant
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1089-8638
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
16
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pubmed:volume |
378
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1040-51
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pubmed:meshHeading |
pubmed-meshheading:18406424-Amino Acid Sequence,
pubmed-meshheading:18406424-Binding Sites,
pubmed-meshheading:18406424-Crystallography, X-Ray,
pubmed-meshheading:18406424-Cytokinins,
pubmed-meshheading:18406424-Lupinus,
pubmed-meshheading:18406424-Molecular Sequence Data,
pubmed-meshheading:18406424-Molecular Structure,
pubmed-meshheading:18406424-Plant Growth Regulators,
pubmed-meshheading:18406424-Plant Proteins,
pubmed-meshheading:18406424-Protein Binding,
pubmed-meshheading:18406424-Protein Folding,
pubmed-meshheading:18406424-Protein Structure, Tertiary,
pubmed-meshheading:18406424-Sequence Alignment,
pubmed-meshheading:18406424-Zeatin
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pubmed:year |
2008
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pubmed:articleTitle |
Lupinus luteus pathogenesis-related protein as a reservoir for cytokinin.
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pubmed:affiliation |
Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, Poland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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