6XWB
Crystal structure of an R-selective transaminase from Thermomyces stellatus.
Summary for 6XWB
| Entry DOI | 10.2210/pdb6xwb/pdb |
| Descriptor | R-selective transaminase, 1,2-ETHANEDIOL, PYRIDOXAL-5'-PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | transaminase, transferase |
| Biological source | Thermomyces stellatus |
| Total number of polymer chains | 2 |
| Total formula weight | 82932.28 |
| Authors | Gourlay, L.J. (deposition date: 2020-01-23, release date: 2020-04-15, Last modification date: 2024-01-24) |
| Primary citation | Heckmann, C.M.,Gourlay, L.J.,Dominguez, B.,Paradisi, F. An ( R )-Selective Transaminase From Thermomyces stellatus : Stabilizing the Tetrameric Form. Front Bioeng Biotechnol, 8:707-707, 2020 Cited by PubMed Abstract: The identification and 3D structural characterization of a homolog of the ()-selective transaminase (RTA) from (RTA), from the thermotolerant fungus (RTA) is here reported. The thermostability of RTA (40% retained activity after 7 days at 40°C) was initially attributed to its tetrameric form in solution, however subsequent studies of RTA revealed it also exists predominantly as a tetramer yet, at 40°C, it is inactivated within 48 h. The engineering of a cysteine residue to promote disulfide bond formation across the dimer-dimer interface stabilized both enzymes, with RTA_G205C retaining almost full activity after incubation at 50°C for 7 days. Thus, the role of this mutation was elucidated and the importance of stabilizing the tetramer for overall stability of RTAs is highlighted. RTA accepts the common amine donors ()-methylbenzylamine, isopropylamine, and d-alanine as well as aromatic and aliphatic ketones and aldehydes. PubMed: 32793563DOI: 10.3389/fbioe.2020.00707 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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