4ynt

Crystal structure of Aspergillus flavus FAD glucose dehydrogenase

spinqualitylabelsall models 4ynt, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ynt is a 1 chain structure with sequence from Aspergillus flavus NRRL3357. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.78Å Ligands: FDA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B8MX95_ASPFN Publication Abstract from PubMed We report the first three-dimensional structure of fungus-derived glucose dehydrogenase using flavin adenine dinucleotide (FAD) as the cofactor. This is currently the most advanced and popular enzyme used in glucose sensor strips manufactured for glycemic control by diabetic patients. We prepared recombinant nonglycosylated FAD-dependent glucose dehydrogenase (FADGDH) derived from Aspergillus flavus (AfGDH) and obtained the X-ray structures of the binary complex of enzyme and reduced FAD at a resolution of 1.78 A and the ternary complex with reduced FAD and D-glucono-1,5-lactone (LGC) at a resolution of 1.57 A. The overall structure is similar to that of fungal glucose oxidases (GOxs) reported till date. The ternary complex with reduced FAD and LGC revealed the residues recognizing the substrate. His505 and His548 were subjected for site-directed mutagenesis studies, and these two residues were revealed to form the catalytic pair, as those conserved in GOxs. The absence of residues that recognize the sixth hydroxyl group of the glucose of AfGDH, and the presence of significant cavity around the active site may account for this enzyme activity toward xylose. The structural information will contribute to the further engineering of FADGDH for use in more reliable and economical biosensing technology for diabetes management. Structural analysis of fungus-derived FAD glucose dehydrogenase.,Yoshida H, Sakai G, Mori K, Kojima K, Kamitori S, Sode K Sci Rep. 2015 Aug 27;5:13498. doi: 10.1038/srep13498. PMID:26311535 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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