Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2049500 | FEBS Letters | 2009 | 4 Pages |
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′.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Naotake Konno, Takuya Ishida, Kiyohiko Igarashi, Shinya Fushinobu, Naoto Habu, Masahiro Samejima, Akira Isogai,