5k3w

Structural characterisation of fold IV-transaminase, CpuTA1, from Curtobacterium pusillum

spinqualitylabelsall models 5k3w, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5k3w is a 2 chain structure with sequence from Curtobacterium pusillum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.503Å Ligands: GAB, PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1S4NYF0_9MICO Publication Abstract from PubMed Transaminases are useful biocatalysts for the production of amino acids and chiral amines as intermediates for a broad range of drugs and fine chemicals. Here, we describe the discovery and characterisation of new transaminases from microorganisms which were enriched in selective media containing (R)-amines as sole nitrogen source. While most of the candidate proteins were clearly assigned to known subgroups of the fold IV family of PLP-dependent enzymes by sequence analysis and characterisation of their substrate specificity, some of them did not fit to any of these groups. The structure of one of these enzymes from Curtobacterium pusillum, which can convert d-amino acids and various (R)-amines with high enantioselectivity, was solved at a resolution of 2.4 A. It shows significant differences especially in the active site compared to other transaminases of the fold IV family and thus indicates the existence of a new subgroup within this family. Although the discovered transaminases were not able to convert ketones in a reasonable time frame, overall, the enrichment-based approach was successful, as we identified two amine transaminases, which convert (R)-amines with high enantioselectivity, and can be used for a kinetic resolution of 1-phenylethylamine and analogues to obtain the (S)-amines with e.e.s >99%. Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold.,Pavkov-Keller T, Strohmeier GA, Diepold M, Peeters W, Smeets N, Schurmann M, Gruber K, Schwab H, Steiner K Sci Rep. 2016 Dec 1;6:38183. doi: 10.1038/srep38183. PMID:27905516 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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