Crystal structures of glycoside hydrolase family 51 α-L-arabinofuranosidase from Thermotoga maritima.
α-L-Arabinofuranosidase from the hyperthermophilic bacterium Thermotoga maritima (Tm-AFase) is an extremely thermophilic enzyme belonging to glycoside hydrolase family 51. It can catalyze the transglycosylation of a novel glycosyl donor, 4,6-dimethoxy-1,3,5-triazin-2-yl (DMT)-β-D-xylopyranoside. In this study we determined the crystal structures of Tm-AFase in substrate-free and complex forms with arabinose and xylose at 1.8-2.3 Å resolution to determine the architecture of the substrate binding pocket. Subsite -1 of Tm-AFase is similar to that of α-L-arabinofuranosidase from Geobacillus stearothermophilus, but the substrate binding pocket of Tm-AFase is narrower and more hydrophobic. Possible substrate binding modes were investigated by automated docking analysis.
Department of Biotechnology, The University of Tokyo, Tokyo, Japan.
Do-Hyun
DH
Im
Kei-ichi
K
Kimura
Fumitaka
F
Hayasaka
Tomonari
T
Tanaka
Masato
M
Noguchi
Atsushi
A
Kobayashi
Shin-ichiro
S
Shoda
Kentaro
K
Miyazaki
Takayoshi
T
Wakagi
Shinya
S
Fushinobu
D001665:Binding Sites; D055162:Biocatalysis; D003460:Crystallization; D018360:Crystallography, X-Ray; D006026:Glycoside Hydrolases / Q000737:chemistry*; D011485:Protein Binding; D020124:Thermotoga maritima / Q000201:enzymology*
D006026:Glycoside Hydrolases; C019713:alpha-N-arabinofuranosidase