Crystal structure of polysaccharide lyase family 20 endo-beta-1,4-glucuronan lyase from the filamentous fungus Trichoderma reesei.
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'.
Konno
Naotake
N
Department of Biomaterials, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Ishida
Takuya
T
Igarashi
Kiyohiko
K
Fushinobu
Shinya
S
Habu
Naoto
N
Samejima
Masahiro
M
Isogai
Akira
A
D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011133:Polysaccharide-Lyases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D011487:Protein Conformation; D014242:Trichoderma / Q000201:enzymology*
D011133:Polysaccharide-Lyases; C109209:glucuronan lyase