Preliminary X-ray crystallographic analysis of a plant defence protein, the polygalacturonase-inhibiting protein from Phaseolus vulgaris.
A leucine-rich repeat plant protein involved in resistance to pathogens, a polygalacturonase-inhibiting protein (PGIP-1) from Phaseolus vulgaris, has been crystallized and preliminary X-ray characterization has been performed. The protein contains ten repeats of a short (24 amino-acid) leucine-rich repeat motif. Single crystals of the protein were grown from vapour-diffusion experiments using PEG 2K monomethylether as precipitant; these crystals diffract to at least 2.3 A resolution. The space group is P2(1), with two molecules of PGIP-1 in the asymmetric unit; the crystals contain approximately 38% solvent.
Leech
A
A
School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, England.
Mattei
B
B
Federici
L
L
De Lorenzo
G
G
Hemmings
A M
AM
D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification*; D007887:Fabaceae / Q000737:chemistry* / Q000235:genetics; D018551:Solanum lycopersicum / Q000235:genetics; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D030821:Plants, Genetically Modified; D010946:Plants, Medicinal; D011096:Polygalacturonase / Q000037:antagonists & inhibitors*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification
D004791:Enzyme Inhibitors; C081479:PGIP protein, plant; D010940:Plant Proteins; D011994:Recombinant Proteins; D011096:Polygalacturonase