1OGQ

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

Summary for 1OGQ

• Entry DOI: 10.2210/pdb1ogq/pdb
• Descriptor: POLYGALACTURONASE INHIBITING PROTEIN, 2-acetamido-2-deoxy-beta-D-glucopyranose, ACETATE ION, ... (4 entities in total)
• Functional Keywords: polygalacturonase inhibiting protein, inhibitor
• Biological source: PHASEOLUS VULGARIS (KIDNEY BEAN)
• Cellular location: Secreted, cell wall: P58822
• Total number of polymer chains: 1
• Total formula weight: 34966.72

Authors

Di Matteo, A.,Federici, L.,Mattei, B.,Salvi, G.,Johnson, K.A.,Savino, C.,De Lorenzo, G.,Tsernoglou, D.,Cervone, F. (deposition date: 2003-05-08, release date: 2003-07-24, Last modification date: 2024-10-23)

Primary citation

Di Matteo, A.,Federici, L.,Mattei, B.,Salvi, G.,Johnson, K.A.,Savino, C.,De Lorenzo, G.,Tsernoglou, D.,Cervone, F.
The Crystal Structure of Polygalacturonase-Inhibiting Protein (Pgip), a Leucine-Rich Repeat Protein Involved in Plant Defense
Proc.Natl.Acad.Sci.USA, 100:10124-, 2003

PubMed 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.

PubMed: 12904578
DOI: 10.1073/PNAS.1733690100

Experimental method

X-RAY DIFFRACTION (1.7 Å)