3ug5 | pdb_00003ug5

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

spinqualitylabelsall models 3ug5, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ug5 is a 6 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: TRS, XYP Related: 3ug3, 3ug4 Gene: TM_0281 (Thermotoga maritima) Activity: Alpha-N-arabinofuranosidase, with EC number 3.2.1.55 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Crystal Structures of Glycoside Hydrolase Family 51 alpha-L-Arabinofuranosidase from Thermotoga maritima.,Im DH, Kimura K, Hayasaka F, Tanaka T, Noguchi M, Kobayashi A, Shoda S, Miyazaki K, Wakagi T, Fushinobu S Biosci Biotechnol Biochem. 2012 Feb 23;76(2):423-8. Epub 2012 Feb 7. PMID:22313787 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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