1HG8

Endopolygalacturonase from the phytopathogenic fungus Fusarium moniliforme

1HG8 の概要

• エントリーDOI: 10.2210/pdb1hg8/pdb
• 分子名称: ENDOPOLYGALACTURONASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: hydrolase, pectin degradation
• 由来する生物種: FUSARIUM MONILIFORME
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36868.10

構造登録者

Federici, L.,Caprari, C.,Mattei, B.,Savino, C.,De Lorenzo, G.,Cervone, F.,Tsernoglou, D. (登録日: 2000-12-13, 公開日: 2001-11-10, 最終更新日: 2024-10-16)

主引用文献

Federici, L.,Caprari, C.,Mattei, B.,Savino, C.,Di Matteo, A.,De Lorenzo, G.,Cervone, F.,Tsernoglou, D.
Structural Requirements of Endopolygalacturonase for the Interaction with Pgip (Polygalacturonase-Inhibiting Protein)
Proc.Natl.Acad.Sci.USA, 98:13425-, 2001

PubMed 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.

PubMed: 11687632
DOI: 10.1073/PNAS.231473698

実験手法

X-RAY DIFFRACTION (1.73 Å)