8HDD
Complex structure of catalytic, small, and a partial electron transfer subunits from Burkholderia cepacia FAD glucose dehydrogenase
Summary for 8HDD
| Entry DOI | 10.2210/pdb8hdd/pdb |
| Related | 6A2U |
| Descriptor | Glucose dehydrogenase, Glucose dehydrogenase beta subunit, Twin-arginine translocation pathway signal, ... (6 entities in total) |
| Functional Keywords | glucose dehydrogenase, fad, burkholderia cepacia, cytochrome c, hem, oxidoreductase |
| Biological source | Burkholderia cepacia More |
| Total number of polymer chains | 3 |
| Total formula weight | 126455.52 |
| Authors | Yoshida, H.,Sode, K. (deposition date: 2022-11-04, release date: 2022-12-14, Last modification date: 2024-11-06) |
| Primary citation | Okuda-Shimazaki, J.,Yoshida, H.,Lee, I.,Kojima, K.,Suzuki, N.,Tsugawa, W.,Yamada, M.,Inaka, K.,Tanaka, H.,Sode, K. Microgravity environment grown crystal structure information based engineering of direct electron transfer type glucose dehydrogenase. Commun Biol, 5:1334-1334, 2022 Cited by PubMed Abstract: The heterotrimeric flavin adenine dinucleotide dependent glucose dehydrogenase is a promising enzyme for direct electron transfer (DET) principle-based glucose sensors within continuous glucose monitoring systems. We elucidate the structure of the subunit interface of this enzyme by preparing heterotrimer complex protein crystals grown under a space microgravity environment. Based on the proposed structure, we introduce inter-subunit disulfide bonds between the small and electron transfer subunits (5 pairs), as well as the catalytic and the electron transfer subunits (9 pairs). Without compromising the enzyme's catalytic efficiency, a mutant enzyme harboring Pro205Cys in the catalytic subunit, Asp383Cys and Tyr349Cys in the electron transfer subunit, and Lys155Cys in the small subunit, is determined to be the most stable of the variants. The developed engineered enzyme demonstrate a higher catalytic activity and DET ability than the wild type. This mutant retains its full activity below 70 °C as well as after incubation at 75 °C for 15 min - much higher temperatures than the current gold standard enzyme, glucose oxidase, is capable of withstanding. PubMed: 36473944DOI: 10.1038/s42003-022-04286-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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