NDLI: The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense.

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The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense.

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The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Di Matteo, A. De Lorenzo, G. Johnson, K. A. Tsernoglou, D. Salvi, G. Cervone, F. Mattei, B. Savino, C. Federici, L.
Description	Author Affiliation: Di Matteo A ( Department of Biochemical Sciences and Consiglio Nazionale delle Ricerche, Institute for Molecular Biology and Pathology, University of Rome La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy.);
Abstract	Polygalacturonase-inhibiting proteins (PGIPs) are plant cell wall proteins that protect plants from fungal invasion. They interact with endopolygalacturonases secreted by phytopathogenic fungi, inhibit their enzymatic activity, and favor the accumulation of oligogalacturonides, which activate plant defense responses. PGIPs are members of the leucine-rich repeat (LRR) protein family that in plants play crucial roles in development, defense against pathogens, and recognition of beneficial microbes. Here we report the crystal structure at 1.7-A resolution of a PGIP from Phaseolus vulgaris. The structure is characterized by the presence of two beta-sheets instead of the single one originally predicted by modeling studies. The structure also reveals a negatively charged surface on the LRR concave face, likely involved in binding polygalacturonases. The structural information on PGIP provides a basis for designing more efficient inhibitors for plant protection.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Phaseolus Chemistry Plant Proteins Amino Acid Sequence Crystallography, X-Ray Enzyme Inhibitors Fungi Enzymology Pathogenicity Genes, Plant Models, Molecular Molecular Sequence Data Genetics Physiology Plant Diseases Microbiology Polygalacturonase Antagonists & Inhibitors Protein Isoforms Protein Structure, Secondary Recombinant Proteins Sequence Homology, Amino Acid Static Electricity Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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