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The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer

Pijning, T., van Pouderoyen, G., Kluskens, L., van der Oost, J. & Dijkstra, B. W., 19-Nov-2009, In : FEBS Letters. 583, 22, p. 3665-3670 6 p.

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DOI

  • Tjaard Pijning
  • Gertie van Pouderoyen
  • Leon Kluskens
  • John van der Oost
  • Bauke W. Dijkstra

The exopolygalacturonase from Thermotoga maritima is the most thermoactive and thermostable pectinase known to date. Here we present its crystal structure at 2.05 angstrom resolution. High structural homology around the active site allowed us to propose a model for substrate binding, explaining the exo-cleavage activity and specificity for non-methylated saturated galacturonate at the non-reducing end. Furthermore, the structure reveals unique features that contribute to the formation of stable tetramers in solution. Such an oligomerization has not been observed before for polygalacturonases. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

Original languageEnglish
Pages (from-to)3665-3670
Number of pages6
JournalFEBS Letters
Volume583
Issue number22
Publication statusPublished - 19-Nov-2009

    Keywords

  • Exopolygalacturonase, X-ray crystallography, Crystal structure, Oligomerization, Thermostability, ACTIVE-SITE, ENDOPOLYGALACTURONASE-I, ASPERGILLUS-ACULEATUS, SEQUENCE ALIGNMENTS, POLYGALACTURONASE, PROTEIN, FEATURES, CRYSTALLOGRAPHY, MUTAGENESIS, FAMILY-28

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