3UG5: Crystal Structure Of Alpha-L-Arabinofuranosidase From Thermotoga Maritima Xylose Complex

Citation:
Abstract
alpha-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)-beta-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 A resolution to determine the architecture of the substrate binding pocket. Subsite -1 of Tm-AFase is similar to that of alpha-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.
PDB ID: 3UG5Download
MMDB ID: 97801
PDB Deposition Date: 2011/11/2
Updated in MMDB: 2012/03
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 3UG5: hexameric; determined by author
Molecular Components in 3UG5
Label Count Molecule
Proteins (6 molecules)
6
Alpha-l-arabinofuranosidase
Molecule annotation
Chemicals (27 molecules)
1
12
2
15
* Click molecule labels to explore molecular sequence information.

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