8H7V

Trans-3/4-proline-hydroxylase H11 with AKG

Summary for 8H7V

• Entry DOI: 10.2210/pdb8h7v/pdb
• Descriptor: Phytanoyl-CoA dioxygenase, 2-OXOGLUTARIC ACID, FE (III) ION, ... (4 entities in total)
• Functional Keywords: l-proline, trans, hydroxylase, akg, hydrolase, structural protein
• Biological source: uncultured bacterium esnapd13
• Total number of polymer chains: 2
• Total formula weight: 60621.46

Authors

Gong, W.M.,Hu, X.Y. (deposition date: 2022-10-21, release date: 2023-04-19, Last modification date: 2024-05-29)

Primary citation

Hu, X.,Huang, X.,Liu, J.,Zheng, P.,Gong, W.,Yang, L.
Structures of L-proline trans-hydroxylase reveal the catalytic specificity and provide deeper insight into AKG-dependent hydroxylation.
Acta Crystallogr D Struct Biol, 79:318-325, 2023

PubMed Abstract: L-Proline hydroxylase is a member of the non-heme Fe/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.

PubMed: 36974966
DOI: 10.1107/S2059798323001936

Experimental method

X-RAY DIFFRACTION (1.97 Å)