Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger

FEBS Letters

van Pouderoyen, Gertie²  Benen, Jacques A.E¹  Dijkstra, Bauke W²  Snijder, Harm J² 

[1] Fungal Genomics, Laboratory of Microbiology, Wageningen University, Dreyenlaan 2, 7603 HA Wageningen, The Netherlands;Laboratory of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands

关键词: Endopolygalacturonase;    Processivity;    X-ray crystallography;    β-Helix;    Aspergillus niger;   

DOI  :  10.1016/S0014-5793(03)01221-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Endopolygalacturonase I is a processive enzyme, while the 60% sequence identical endopolygalacturonase II is not. The 1.70 Å 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.

【 授权许可】

Unknown