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Crystal structure of polysaccharide lyase family 20 endo‐β‐1,4‐glucuronan lyase from the filamentous fungus Trichoderma reesei
Author(s) -
Konno Naotake,
Ishida Takuya,
Igarashi Kiyohiko,
Fushinobu Shinya,
Habu Naoto,
Samejima Masahiro,
Isogai Akira
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.03.034
Subject(s) - trichoderma reesei , lyase , glycoside hydrolase , chemistry , enzyme , biochemistry , hydrolase , polysaccharide , stereochemistry , cellulase
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′.