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Crystal structure of endo-beta-1,4-glucuronan lyase from fungus Trichoderma reeseiCrystal structure of endo-beta-1,4-glucuronan lyase from fungus Trichoderma reesei
Structural highlights
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 PubMedThe crystal structure of endo-beta-(1-->4)-glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8A resolution as the first three-dimensional structure of polysaccharide lyase (PL) family 20. TrGL has a typical beta-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'. Crystal structure of polysaccharide lyase family 20 endo-beta-1,4-glucuronan lyase from the filamentous fungus Trichoderma reesei.,Konno N, Ishida T, Igarashi K, Fushinobu S, Habu N, Samejima M, Isogai A FEBS Lett. 2009 Apr 17;583(8):1323-6. Epub 2009 Mar 22. PMID:19306878[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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