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6GHW

Substituting the prolines of 4-oxalocrotonate tautomerase with non-canonical analogue (2S)-3,4-dehydroproline

Summary for 6GHW
Entry DOI10.2210/pdb6ghw/pdb
Descriptor2-hydroxymuconate tautomerase, CALCIUM ION (3 entities in total)
Functional Keywordsnon-canonical amino acid, (2s)-3, 4-dehydroproline, isomerase
Biological sourcePseudomonas putida
Total number of polymer chains3
Total formula weight20493.51
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 citationLukesch, 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: 30804446
DOI: 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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