8hdd

Complex structure of catalytic, small, and a partial electron transfer subunits from Burkholderia cepacia FAD glucose dehydrogenase

spinqualitylabelsall models 8hdd, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8hdd is a 3 chain structure with sequence from Burkholderia cepacia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: FAD, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8GQE7_BURCE Publication Abstract from PubMed 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 degrees C as well as after incubation at 75 degrees C for 15 min - much higher temperatures than the current gold standard enzyme, glucose oxidase, is capable of withstanding. Microgravity environment grown crystal structure information based engineering of direct electron transfer type glucose dehydrogenase.,Okuda-Shimazaki J, Yoshida H, Lee I, Kojima K, Suzuki N, Tsugawa W, Yamada M, Inaka K, Tanaka H, Sode K Commun Biol. 2022 Dec 6;5(1):1334. doi: 10.1038/s42003-022-04286-9. PMID:36473944 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA