Crystal structure of polysaccharide lyase family 20 endo‐β‐1,4‐glucuronan lyase from the filamentous fungus Trichoderma reesei
Open Access
- 21 March 2009
- journal article
- Published by Wiley in FEBS Letters
- Vol. 583 (8), 1323-1326
- https://doi.org/10.1016/j.febslet.2009.03.034
Abstract
The crystal structure of endo‐β‐(1→4)‐glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8 Å resolution as the first three‐dimensional structure of polysaccharide lyase (PL) family 20. TrGL has a typical β‐jelly roll fold, which is similar to glycoside hydrolase family 16 and PL7 enzymes. A calcium ion is bound to the site far from the cleft and appears to contribute to the stability. There are several completely conserved residues in the cleft. Possible catalytic residues are predicted based on structural comparison with PL7 alginate lyase A1–II′.This publication has 23 references indexed in Scilit:
- Crystal Structure of Glycoside Hydrolase Family 55 β-1,3-Glucanase from the Basidiomycete Phanerochaete chrysosporiumOnline Journal of Public Health Informatics, 2009
- Cloning of the Trichoderma reesei cDNA Encoding a Glucuronan Lyase Belonging to a Novel Polysaccharide Lyase FamilyApplied and Environmental Microbiology, 2009
- The Carbohydrate-Active EnZymes database (CAZy): an expert resource for GlycogenomicsNucleic Acids Research, 2008
- Substrate recognition by family 7 alginate lyase from Sphingomonas sp. A1Journal of Molecular Biology, 2008
- Coot: model-building tools for molecular graphicsActa crystallographica. Section D, Structural biology, 2004
- High-resolution Crystal Structure of Arthrobacter aurescens Chondroitin AC Lyase: An Enzyme–Substrate Complex Defines the Catalytic MechanismJournal of Molecular Biology, 2004
- vAL-1, a novel polysaccharide lyase encoded by chlorovirus CVK2FEBS Letters, 2004
- Crystal structure of alginate lyase A1-III complexed with trisaccharide product at 2.0 Å resolutionJournal of Molecular Biology, 2001
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa crystallographica. Section D, Structural biology, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modeMethods in Enzymology, 1997