7F2V
Urate oxidase from Thermobispora bispora in apo form
Summary for 7F2V
Entry DOI | 10.2210/pdb7f2v/pdb |
Descriptor | Uricase, SULFATE ION, DIMETHYL SULFOXIDE, ... (4 entities in total) |
Functional Keywords | uricase, urate oxidase, oxidoreductase |
Biological source | Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / NBRC 14880 / R51) |
Total number of polymer chains | 2 |
Total formula weight | 68628.77 |
Authors | Chiu, Y.C.,Hsu, T.S.,Huang, C.Y.,Hsu, C.H. (deposition date: 2021-06-14, release date: 2022-05-04, Last modification date: 2023-11-29) |
Primary citation | Chiu, Y.C.,Hsu, T.S.,Huang, C.Y.,Hsu, C.H. Structural and biochemical insights into a hyperthermostable urate oxidase from Thermobispora bispora for hyperuricemia and gout therapy. Int.J.Biol.Macromol., 188:914-923, 2021 Cited by PubMed Abstract: Microbial urate oxidase has emerged as a potential source of therapeutic properties for hyperuricemia in arthritic gout and renal disease. The thermostability and long-term thermal tolerance of the enzyme need to be established to prolong its therapeutic effects. Here, we present the biochemical and structural aspects of a hyperthermostable urate oxidase (TbUox) from the thermophilic microorganism Thermobispora bispora. Enzymatic characterization of TbUox revealed that it was active over a wide range of temperatures, from 30 to 70 °C, with optimal activity at 65 °C and pH 8.0, which suggests its applicability under physiological conditions. Moreover, TbUox exhibits high thermostability from 10 to 65 °C, with Tm of 70.3 °C and near-neutral pH stability from pH 7.0 to 8.0 and high thermal tolerance. The crystal structures of TbUox revealed a distinct feature of the C-terminal loop extensions that may help with protein stability via inter-subunit interactions. In addition, the high thermal tolerance of TbUox may be contributed by the extensive inter-subunit contacts via salt bridges, hydrogen bonds, and hydrophobic interactions. The findings in this study provide a molecular basis for the thermophilic TbUox urate oxidase for application in hyperuricemia and gout therapy. PubMed: 34403675DOI: 10.1016/j.ijbiomac.2021.08.081 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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