3UG5

Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex

Summary for 3UG5

• Entry DOI: 10.2210/pdb3ug5/pdb
• Related: 3UG3 3UG4
• Descriptor: Alpha-L-arabinofuranosidase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, beta-D-xylopyranose, ... (4 entities in total)
• Functional Keywords: tim barrel, hydrolase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 6
• Total formula weight: 348152.66

Authors

Im, D.-H.,Miyazaki, K.,Wakagi, T.,Fushinobu, S. (deposition date: 2011-11-02, release date: 2012-03-07, Last modification date: 2023-11-01)

Primary citation

Im, D.-H.,Kimura, K.I.,Hayasaka, F.,Tanaka, T.,Noguchi, M.,Kobayashi, A.,Shoda, S.,Miyazaki, K.,Wakagi, T.,Fushinobu, S.
Crystal Structures of Glycoside Hydrolase Family 51 alpha-L-Arabinofuranosidase from Thermotoga maritima
Biosci.Biotechnol.Biochem., 76:423-428, 2012

PubMed Abstract: 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.

PubMed: 22313787
DOI: 10.1271/bbb.110902

Experimental method

X-RAY DIFFRACTION (2.3 Å)