6C3C
PLP-dependent L-arginine hydroxylase RohP quinonoid I complex
Summary for 6C3C
| Entry DOI | 10.2210/pdb6c3c/pdb |
| Descriptor | Uncharacterized protein, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (5 entities in total) |
| Functional Keywords | o2-, plp-dependent hydroxylase, biosynthetic protein |
| Biological source | Streptomyces cattleya |
| Total number of polymer chains | 2 |
| Total formula weight | 96269.02 |
| Authors | Hedges, J.B.,Ryan, K.S. (deposition date: 2018-01-09, release date: 2018-03-07, Last modification date: 2023-10-04) |
| Primary citation | Hedges, J.B.,Kuatsjah, E.,Du, Y.L.,Eltis, L.D.,Ryan, K.S. Snapshots of the Catalytic Cycle of an O2, Pyridoxal Phosphate-Dependent Hydroxylase. ACS Chem. Biol., 13:965-974, 2018 Cited by PubMed Abstract: Enzymes that catalyze hydroxylation of unactivated carbons normally contain heme and nonheme iron cofactors. By contrast, how a pyridoxal phosphate (PLP)-dependent enzyme could catalyze such a hydroxylation was unknown. Here, we investigate RohP, a PLP-dependent enzyme that converts l-arginine to ( S)-4-hydroxy-2-ketoarginine. We determine that the RohP reaction consumes oxygen with stoichiometric release of HO. To understand this unusual chemistry, we obtain ∼1.5 Å resolution structures that capture intermediates along the catalytic cycle. Our data suggest that RohP carries out a four-electron oxidation and a stereospecific alkene hydration to give the ( S)-configured product. Together with our earlier studies on an O, PLP-dependent l-arginine oxidase, our work suggests that there is a shared pathway leading to both oxidized and hydroxylated products from l-arginine. PubMed: 29466666DOI: 10.1021/acschembio.8b00039 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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