Abstract
The pathogenesis-related protein of the PR10 class from Lupinus luteus (yellow lupin), LlPR10.1A, is constitutively expressed in roots. It is also accumulated in leaves treated with a suspension of pathogenic bacteria as a response to stress. Recombinant yellow-lupin LlPR10.1A protein has been overexpressed in Escherichia coli as a fusion product with maltose-binding protein. LlPR10.1A crystallizes in the orthorhombic P2(1)2(1)2(1) space group and the crystals diffract to 2.45 A resolution. The structure has been solved by molecular replacement, using the structure of a birch-pollen allergen protein as a model.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ATP-Binding Cassette Transporters*
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Allergens*
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Antigens, Plant
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Crystallization
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Crystallography, X-Ray
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Escherichia coli
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Escherichia coli Proteins*
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Fabaceae
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Maltose-Binding Proteins
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Models, Molecular
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Monosaccharide Transport Proteins*
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Plant Proteins / chemistry*
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Plant Proteins / genetics
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Plants, Medicinal
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Protein Folding
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
Substances
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ATP-Binding Cassette Transporters
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Allergens
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Antigens, Plant
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Carrier Proteins
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Escherichia coli Proteins
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Maltose-Binding Proteins
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Monosaccharide Transport Proteins
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Plant Proteins
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Recombinant Fusion Proteins
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maltose transport system, E coli
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pathogenesis-related proteins, plant
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Bet v 1 allergen, Betula