3JUR

The crystal structure of a hyperthermoactive Exopolygalacturonase from Thermotoga maritima

3JUR の概要

• エントリーDOI: 10.2210/pdb3jur/pdb
• 分子名称: Exo-poly-alpha-D-galacturonosidase (2 entities in total)
• 機能のキーワード: beta-helix, cell wall biogenesis/degradation, glycosidase, hydrolase
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 202250.76

構造登録者

Pijning, T.,van Pouderoyen, G.,Kluskens, L.D.,van der Oost, J.,Dijkstra, B.W. (登録日: 2009-09-15, 公開日: 2009-11-17, 最終更新日: 2023-11-01)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.05 Å)