research papers
L-Proline hydroxylase is a member of the non-heme Fe2+/α-ketoglutarate (AKG)-dependent hydroxylase family that catalyzes the reaction from L-proline to hydroxy-L-proline, which is widely used in drug synthesis, biochemistry, food supplementation and cosmetic industries. Here, the first crystal structure of L-proline trans-hydroxylase and its complexes with substrate and product are reported, which reveal the structural basis of trans–cis proline hydroxylation selectivity. Structure comparison with other AKG-dependent hydroxylases identifies conserved amino acid residues, which may serve as signatures of in-line or off-line AKG binding modes in the AKG-dependent enzyme family.
Keywords: AKG-dependent hydroxylases; hydroxy-L-proline; L-proline trans-hydroxylases; trans–cis proline hydroxylation selectivity; catalytic specificity; AKG binding modes.
Supporting information
Portable Document Format (PDF) file https://doi.org/10.1107/S2059798323001936/di5060sup1.pdf |
PDB references: trans-3/4-proline-hydroxylase H11 with 4-hydroxyproline, 8h81; trans-3/4-proline-hydroxylase H11 apo structure, 8h7t; trans-3/4-proline-hydroxylase H11 with AKG and L-proline, 8h7y; trans-3/4-proline-hydroxylase H11 with AKG, 8h7v; trans-3/4-proline-hydroxylase H11 with 3-hydroxyproline, 8h85