| Literature DB >> 19306878 |
Naotake Konno1, Takuya Ishida, Kiyohiko Igarashi, Shinya Fushinobu, Naoto Habu, Masahiro Samejima, Akira Isogai.
Abstract
The 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'.Entities:
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Year: 2009 PMID: 19306878 DOI: 10.1016/j.febslet.2009.03.034
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124