Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger

G. van Pouderoyen, H.J. Snijder, J.A.E. Benen, B.W. Dijkstra

Research output: Contribution to journalArticleAcademicpeer-review

71 Citations (Scopus)

Abstract

Endopolygalacturonase I is a processive enzyme, while the 60% sequence identical endopolygalacturonase II is not. The 1.70 Angstrom 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. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Original languageEnglish
Pages (from-to)462-466
JournalFEBS Letters
Volume554
DOIs
Publication statusPublished - 2003

Keywords

  • site-directed mutagenesis
  • acid-sequence similarities
  • crystal-structure
  • crystallographic evidence
  • angstrom resolution
  • protein
  • complex
  • polygalacturonase
  • classification
  • identification

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