1NHC

Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger

1NHC の概要

• エントリーDOI: 10.2210/pdb1nhc/pdb
• 関連するPDBエントリー: 1CZF
• 分子名称: Polygalacturonase I, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• 機能のキーワード: beta-helix, hydrolase
• 由来する生物種: Aspergillus niger
• 細胞内の位置: Secreted (Probable): P26213
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 216075.80

構造登録者

van Pouderoyen, G.,Snijder, H.J.,Benen, J.A.,Dijkstra, B.W. (登録日: 2002-12-19, 公開日: 2003-11-25, 最終更新日: 2024-12-25)

主引用文献

van Pouderoyen, G.,Snijder, H.J.,Benen, J.A.,Dijkstra, B.W.
Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger.
Febs Lett., 554:462-466, 2003

PubMed Abstract: Endopolygalacturonase I is a processive enzyme, while the 60% sequence identical endopolygalacturonase II is not. The 1.70 A resolution crystal structure of endopolygalacturonase I reveals a narrowed substrate binding cleft. In addition, Arg96, a residue in this cleft previously shown to be critical for processivity, interacts with the substrate mimics glycerol and sulfate in several well-defined conformations in the six molecules in the asymmetric unit. From this we conclude that both Arg96 and the narrowed substrate binding cleft contribute to retaining the substrate while it moves through the active site after a cleavage event has occurred.

PubMed: 14623112
DOI: 10.1016/S0014-5793(03)01221-3

実験手法

X-RAY DIFFRACTION (1.7 Å)