4C2L

Crystal structure of endo-xylogalacturonan hydrolase from Aspergillus tubingensis

4C2L の概要

• エントリーDOI: 10.2210/pdb4c2l/pdb
• 分子名称: ENDO-XYLOGALACTURONAN HYDROLASE A, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose, ... (7 entities in total)
• 機能のキーワード: hydrolase, polygalacturonan, gh28
• 由来する生物種: ASPERGILLUS TUBINGENSIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41748.83

構造登録者

Rozeboom, H.J.,Beldman, G.,Schols, H.A.,Dijkstra, B.W. (登録日: 2013-08-19, 公開日: 2013-09-25, 最終更新日: 2024-10-23)

主引用文献

Rozeboom, H.J.,Beldman, G.,Schols, H.A.,Dijkstra, B.W.
Crystal Structure of Endo-Xylogalacturonan Hydrolase from Aspergillus Tubingensis.
FEBS J., 280:6061-, 2013

PubMed Abstract: Endo-xylogalacturonan hydrolase is a member of glycoside hydrolase family 28 (GH28) that hydrolyzes the glycosidic bond between two β-xylose-substituted galacturonic acid residues in pectin. Presented here is the X-ray crystal structure of the endo-xylogalacturonan hydrolase from Aspergillus tubingensis (XghA) at 1.75 Å resolution. The high degree of structural conservation in the active site and catalytic apparatus compared with polygalacturonases indicates that cleavage of the substrate proceeds in essentially the same way as found for the other GH28 enzymes. Molecular modeling of a xylosylated tri-galacturonate in the active site identified the amino acid residues involved in substrate binding. They border a substrate-binding cleft that is much wider than in other polygalacturonases, and can accommodate xylosylated substrates. The most extensive interactions appear to occur at subsite +2, in agreement with the enzyme kinetics results, which showed enhanced activity on substrates with a xylose attached to the galacturonic acid bound at subsite +2.

PubMed: 24034788
DOI: 10.1111/FEBS.12524

実験手法

X-RAY DIFFRACTION (1.75 Å)