Structural highlights
Function
Q9WYR8_THEMA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The exopolygalacturonase from Thermotoga maritima is the most thermoactive and thermostable pectinase known to date. Here we present its crystal structure at 2.05A 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.
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 BW FEBS Lett. 2009 Nov 19;583(22):3665-70. Epub 2009 Oct 23. PMID:19854184[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pijning T, van Pouderoyen G, Kluskens L, van der Oost J, Dijkstra BW. The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer. FEBS Lett. 2009 Nov 19;583(22):3665-70. Epub 2009 Oct 23. PMID:19854184 doi:10.1016/j.febslet.2009.10.047
