Abstract
Acid invertases catalyzing the breakdown of sucrose are regulated at the post-translational level by extracellular inhibitory proteins of 16-20 kDa molecular weight in a pH-dependent manner. Little is known about the characteristics of the underlying protein-protein interaction. Here, the expression, purification, characterization, crystallization and initial X-ray analysis of a biologically active invertase inhibitor Nt-CIF from tobacco is reported. Four crystal forms covering a wide pH range have been obtained and data sets at resolutions higher than 2.5 A have been collected.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cloning, Molecular
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Crystallography, X-Ray
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / metabolism
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Enzyme Inhibitors / pharmacology
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Gene Expression
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Nicotiana / chemistry*
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Plant Proteins / biosynthesis*
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Plant Proteins / chemistry*
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Plant Proteins / genetics
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Plant Proteins / pharmacology
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Recombinant Fusion Proteins / biosynthesis
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / pharmacology
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beta-Fructofuranosidase / antagonists & inhibitors
Substances
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Enzyme Inhibitors
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INH protein, Nicotiana tabacum
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Plant Proteins
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Recombinant Fusion Proteins
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beta-Fructofuranosidase