3JUR

The crystal structure of a hyperthermoactive Exopolygalacturonase from Thermotoga maritima

Summary for 3JUR

Entry DOI	10.2210/pdb3jur/pdb
Descriptor	Exo-poly-alpha-D-galacturonosidase (2 entities in total)
Functional Keywords	beta-helix, cell wall biogenesis/degradation, glycosidase, hydrolase
Biological source	Thermotoga maritima
Total number of polymer chains	4
Total formula weight	202250.76
Authors	Pijning, T.,van Pouderoyen, G.,Kluskens, L.D.,van der Oost, J.,Dijkstra, B.W. (deposition date: 2009-09-15, release date: 2009-11-17, Last modification date: 2023-11-01)
Primary citation	Pijning, T.,van Pouderoyen, G.,Kluskens, L.,van der Oost, J.,Dijkstra, B.W. The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer Febs Lett., 2009 Cited by PubMed Abstract: 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. PubMed: 19854184 DOI: 10.1016/j.febslet.2009.10.047 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.05 Å)

Structure validation