The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramerPijning, 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.
Research output: Contribution to journal › Article › Academic › peer-review
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.
|Number of pages||6|
|Publication status||Published - 19-Nov-2009|
- Exopolygalacturonase, X-ray crystallography, Crystal structure, Oligomerization, Thermostability, ACTIVE-SITE, ENDOPOLYGALACTURONASE-I, ASPERGILLUS-ACULEATUS, SEQUENCE ALIGNMENTS, POLYGALACTURONASE, PROTEIN, FEATURES, CRYSTALLOGRAPHY, MUTAGENESIS, FAMILY-28