6GHW
Substituting the prolines of 4-oxalocrotonate tautomerase with non-canonical analogue (2S)-3,4-dehydroproline
Summary for 6GHW
Entry DOI | 10.2210/pdb6ghw/pdb |
Descriptor | 2-hydroxymuconate tautomerase, CALCIUM ION (3 entities in total) |
Functional Keywords | non-canonical amino acid, (2s)-3, 4-dehydroproline, isomerase |
Biological source | Pseudomonas putida |
Total number of polymer chains | 3 |
Total formula weight | 20493.51 |
Authors | Pavkov-Keller, T.,Lukesch, M.S.,Wiltschi, B.,Gruber, K. (deposition date: 2018-05-09, release date: 2019-03-06, Last modification date: 2024-01-17) |
Primary citation | Lukesch, M.S.,Pavkov-Keller, T.,Gruber, K.,Zangger, K.,Wiltschi, B. Substituting the catalytic proline of 4-oxalocrotonate tautomerase with non-canonical analogues reveals a finely tuned catalytic system. Sci Rep, 9:2697-2697, 2019 Cited by PubMed Abstract: The enzyme 4-oxalocrotonate tautomerase shows remarkable catalytic versatility due to the secondary amine of its N-terminal proline moiety. In this work, we incorporated a range of proline analogues into the enzyme and examined the effects on structure and activity. While the structure of the enzyme remained unperturbed, its promiscuous Michael-type activity was severely affected. This finding demonstrates how atomic changes in a biocatalytic system can abolish its activity. Our work provides a toolbox for successful generation of enzyme variants with non-canonical catalytic proline analogues. PubMed: 30804446DOI: 10.1038/s41598-019-39484-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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