1hg8 Citations

Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein).

Proc. Natl. Acad. Sci. U.S.A. 98 13425-30 (2001)
Cited: 74 times
EuropePMC logo PMID: 11687632

Abstract

To invade a plant tissue, phytopathogenic fungi produce several cell wall-degrading enzymes; among them, endopolygalacturonase (PG) catalyzes the fragmentation and solubilization of homogalacturonan. Polygalacturonase-inhibiting proteins (PGIPs), found in the cell wall of many plants, counteract fungal PGs by forming specific complexes with them. We report the crystal structure at 1.73 A resolution of PG from the phytopathogenic fungus Fusarium moniliforme (FmPG). The structure of FmPG was useful to study the mode of interaction of the enzyme with PGIP-2 from Phaseolus vulgaris. Several amino acids of FmPG were mutated, and their contribution to the formation of the complex with PGIP-2 was investigated by surface plasmon resonance. The residues Lys-269 and Arg-267, located inside the active site cleft, and His-188, at the edge of the active site cleft, are critical for the formation of the complex, which is consistent with the observed competitive inhibition of the enzyme played by PGIP-2. The replacement of His-188 with a proline or the insertion of a tryptophan after position 270, variations that both occur in plant PGs, interferes with the formation of the complex. We suggest that these variations are important structural requirements of plant PGs to prevent PGIP binding.

Articles - 1hg8 mentioned but not cited (7)

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Reviews citing this publication (9)

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Related citations provided by authors (1)

  1. Crystallization and preliminary X-ray diffraction study of the endo-polygalacturonase from Fusarium moniliforme.. Federici L, Mattei B, Caprari C, Savino C, Cervone F, Tsernoglou D Acta Crystallogr. D Biol. Crystallogr. 55 1359-61 (1999)