Secondary Structure and Post-Translational Modifications of the Leucine-Rich Repeat Protein PGIP (Polygalacturonase-Inhibiting Protein) from Phaseolus vulgaris

A detailed analysis of the secondary structure has been carried out on the polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris, a leucine-rich repeat (LRR) protein present in the cell wall of many plants. Far-UV CD and infrared spectroscopies coupled to constrained secondary structur...

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Bibliographic Details
Published in:Biochemistry (Easton) 2001-01, Vol.40 (2), p.569-576
Main Authors: Mattei, Benedetta, Bernalda, Maria Scala, Federici, Luca, Roepstorff, Peter, Cervone, Felice, Boffi, Alberto
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Circular Dichroism
Disulfides - chemistry
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - metabolism
Fabaceae
Glycosylation
Leucine - metabolism
Molecular Sequence Data
Plant Proteins - chemistry
Plant Proteins - metabolism
Plants, Medicinal
Polygalacturonase - antagonists & inhibitors
Protein Processing, Post-Translational
Protein Structure, Secondary
Repetitive Sequences, Amino Acid
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spectroscopy, Fourier Transform Infrared
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Summary:A detailed analysis of the secondary structure has been carried out on the polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris, a leucine-rich repeat (LRR) protein present in the cell wall of many plants. Far-UV CD and infrared spectroscopies coupled to constrained secondary structure prediction methods indicated the presence of 12 α- and 12 β-segments, thus allowing a schematic representation of three domains of the protein, namely, the central LRR region and the two cysteine-rich flanking domains. Peptides from endoproteinase-degraded PGIP were analyzed by mass spectrometry, and four disulfide bonds were identified. Mass spectrometric analysis in combination with glycosidase treatments revealed two N-linked oligosaccharides located on Asn 64 and Asn 141. The main structure resembled the typical complex plant N-glycan consisting of a core pentasaccharide β1,2-xylosylated, carrying an α1,3-fucose linked to the innermost N-acetylglucosamine and one outer arm N-acetylglucosamine residue. The schematic representation of PGIP structural domains is discussed in the framework of the structure and function of LRR proteins.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi0017632