4YNT

Crystal structure of Aspergillus flavus FAD glucose dehydrogenase

Summary for 4YNT

• Entry DOI: 10.2210/pdb4ynt/pdb
• Related: 4YNU
• Descriptor: Glucose oxidase, putative, DIHYDROFLAVINE-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: glucose dehydrogenase, fad, oxidoreductase
• Biological source: Aspergillus flavus NRRL3357
• Total number of polymer chains: 1
• Total formula weight: 62336.49

Authors

Yoshida, H.,Sakai, G.,Kojima, K.,Kamitori, S.,Sode, K. (deposition date: 2015-03-11, release date: 2015-09-02, Last modification date: 2023-11-08)

Primary citation

Yoshida, H.,Sakai, G.,Mori, K.,Kojima, K.,Kamitori, S.,Sode, K.
Structural analysis of fungus-derived FAD glucose dehydrogenase
Sci Rep, 5:13498-13498, 2015

PubMed Abstract: 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 Å and the ternary complex with reduced FAD and D-glucono-1,5-lactone (LGC) at a resolution of 1.57 Å. 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.

PubMed: 26311535
DOI: 10.1038/srep13498

Experimental method

X-RAY DIFFRACTION (1.78 Å)