2W5N

Native structure of the GH93 alpha-L-arabinofuranosidase of Fusarium graminearum

2W5N の概要

• エントリーDOI: 10.2210/pdb2w5n/pdb
• 関連するPDBエントリー: 2W5O
• 分子名称: ALPHA-L-ARABINOFURANOSIDASE, 1,2-ETHANEDIOL, TRIETHYLENE GLYCOL, ... (5 entities in total)
• 機能のキーワード: hydrolase, alpha-l-arabinofuranosidase, glycosyl hydrolase, gh93
• 由来する生物種: GIBBERELLA ZEAE
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41426.68

構造登録者

Carapito, R.,Imberty, A.,Jeltsch, J.M.,Byrns, S.C.,Tam, P.H.,Lowary, T.L.,Varrot, A.,Phalip, V. (登録日: 2008-12-11, 公開日: 2009-03-03, 最終更新日: 2024-05-01)

主引用文献

Carapito, R.,Imberty, A.,Jeltsch, J.M.,Byrns, S.C.,Tam, P.H.,Lowary, T.L.,Varrot, A.,Phalip, V.
Molecular Basis of Arabinobio-Hydrolase Activity in Phytopathogenic Fungi. Crystal Structure and Catalytic Mechanism of Fusarium Graminearum Gh93 Exo-Alpha-L-Arabinanase.
J.Biol.Chem., 284:12285-, 2009

PubMed Abstract: The phytopathogenic fungus Fusarium graminearum secretes a very diverse pool of glycoside hydrolases (GHs) aimed at degrading plant cell walls. alpha-l-Arabinanases are essential GHs participating in the complete hydrolysis of hemicellulose, a natural resource for various industrial processes, such as bioethanol or pharmaceuticals production. Arb93A, the exo-1,5-alpha-l-arabinanase of F. graminearum encoded by the gene fg03054.1, belongs to the GH93 family, for which no structural data exists. The enzyme is highly active (1065 units/mg) and displays a strict substrate specificity for linear alpha-1,5-l-arabinan. Biochemical assays and NMR experiments demonstrated that the enzyme releases alpha-1,5-l-arabinobiose from the nonreducing end of the polysaccharide. We determined the crystal structure of the native enzyme and its complex with alpha-1,5-l-arabinobiose, a degradation product of alpha-Me-1,5-l-arabinotetraose, at 1.85 and 2.05A resolution, respectively. Arb93A is a monomeric enzyme, which presents the six-bladed beta-propeller fold characteristic of sialidases of clan GHE. The configuration of the bound arabinobiose is consistent with the retaining mechanism proposed for the GH93 family. Catalytic residues were proposed from the structural analysis, and site-directed mutagenesis was used to validate their role. They are significantly different from those observed for GHE sialidases.

PubMed: 19269961
DOI: 10.1074/JBC.M900439200

実験手法

X-RAY DIFFRACTION (1.85 Å)