1hg8
From Proteopedia
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ENDOPOLYGALACTURONASE FROM THE PHYTOPATHOGENIC FUNGUS FUSARIUM MONILIFORME
Overview
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.
About this Structure
1HG8 is a Single protein structure of sequence from Gibberella moniliformis with NAG as ligand. Full crystallographic information is available from OCA.
Reference
Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein)., Federici L, Caprari C, Mattei B, Savino C, Di Matteo A, De Lorenzo G, Cervone F, Tsernoglou D, Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):13425-30. Epub 2001 Oct 30. PMID:11687632
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