6FYQ
The crystal structure of a new transaminase from the marine bacterium Virgibacillus
Summary for 6FYQ
| Entry DOI | 10.2210/pdb6fyq/pdb |
| Descriptor | amine transaminase, PYRIDOXAL-5'-PHOSPHATE, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | omega-amino acid-pyruvate aminotransferase, virgibacillus pantothenticus, transferase |
| Biological source | Virgibacillus pantothenticus |
| Total number of polymer chains | 1 |
| Total formula weight | 53710.58 |
| Authors | Gourlay, L.J. (deposition date: 2018-03-12, release date: 2018-12-12, Last modification date: 2024-01-17) |
| Primary citation | Guidi, B.,Planchestainer, M.,Contente, M.L.,Laurenzi, T.,Eberini, I.,Gourlay, L.J.,Romano, D.,Paradisi, F.,Molinari, F. Strategic single point mutation yields a solvent- and salt-stable transaminase from Virgibacillus sp. in soluble form. Sci Rep, 8:16441-16441, 2018 Cited by PubMed Abstract: A new transaminase (VbTA) was identified from the genome of the halotolerant marine bacterium Virgibacillus 21D. Following heterologous expression in Escherichia coli, it was located entirely in the insoluble fraction. After a single mutation, identified via sequence homology analyses, the VbTA T16F mutant was successfully expressed in soluble form and characterised. VbTA T16F showed high stability towards polar organic solvents and salt exposure, accepting mainly hydrophobic aromatic amine and carbonyl substrates. The 2.0 Å resolution crystal structure of VbTA T16F is here reported, and together with computational calculations, revealed that this mutation is crucial for correct dimerisation and thus correct folding, leading to soluble protein expression. PubMed: 30401905DOI: 10.1038/s41598-018-34434-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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