Crystal structure of polysaccharide lyase family 20 endo-β-1,4-glucuronan lyase from the filamentous fungus Trichoderma reesei

Konno, Naotake; Ishida, Takuya; Igarashi, Kiyohiko; Fushinobu, Shinya; Habu, Naoto; Samejima, Masahiro; Isogai, Akira

doi:10.1016/j.febslet.2009.03.034

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Volume 583, Issue 8 , Pages 1323-1326, 17 April 2009

Crystal structure of polysaccharide lyase family 20 endo-β-1,4-glucuronan lyase from the filamentous fungus Trichoderma reesei

Edited by Richard Cogdell

Naotake Konno
- Department of Biomaterials, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan
- These authors contributed equally to this work.
Takuya Ishida
- Department of Biomaterials, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan
- These authors contributed equally to this work.
Kiyohiko Igarashi
- Department of Biomaterials, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan
Shinya Fushinobu
- Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan
- Corresponding author. Fax: +81 3 5841 5151.
Naoto Habu
- Department of Bioproductive Science, Utsunomiya University, 350 Mine-machi, Utsunomiya, Tochigi 321-8505, Japan
Masahiro Samejima
- Department of Biomaterials, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan
Akira Isogai
- Department of Biomaterials, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan

Received 24 February 2009; received in revised form 11 March 2009; accepted 16 March 2009. published online 23 March 2009.

Abstract

The crystal structure of endo-β-(1→4)-glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8Å 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′.