8h85 | pdb_00008h85

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

spinqualitylabelsall models 8h85, resolution 2.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8h85 is a 1 chain structure with sequence from Uncultured bacterium esnapd13. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.38Å Ligands: HY3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function S5TUM1_9BACT Publication Abstract from PubMed L-Proline hydroxylase is a member of the non-heme Fe(2+)/alpha-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. Structures of L-proline trans-hydroxylase reveal the catalytic specificity and provide deeper insight into AKG-dependent hydroxylation.,Hu X, Huang X, Liu J, Zheng P, Gong W, Yang L Acta Crystallogr D Struct Biol. 2023 Apr 1;79(Pt 4):318-325. doi: , 10.1107/S2059798323001936. Epub 2023 Mar 28. PMID:36974966 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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