6c3a | pdb_00006c3a

O2-, PLP-dependent L-arginine hydroxylase RohP 4-hydroxy-2-ketoarginine complex

spinqualitylabelsall models 6c3a, resolution 1.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6c3a is a 2 chain structure with sequence from Streptomyces cattleya NRRL 8057 = DSM 46488. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.53Å Ligands: EDO, EGV, LLP, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G8WNK6_STREN Publication Abstract from PubMed 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 H2O2. To understand this unusual chemistry, we obtain approximately 1.5 A 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 O2, PLP-dependent l-arginine oxidase, our work suggests that there is a shared pathway leading to both oxidized and hydroxylated products from l-arginine. Snapshots of the Catalytic Cycle of an O2, Pyridoxal Phosphate-Dependent Hydroxylase.,Hedges JB, Kuatsjah E, Du YL, Eltis LD, Ryan KS ACS Chem Biol. 2018 Feb 28. doi: 10.1021/acschembio.8b00039. PMID:29466666 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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