of the tested peptides, six or more residues are required for efficient hydroxylation. Hydroxylation is ablated when the C-terminus is extended to more closely resemble a protein. Hydroxylation occurs with incorporation of more than 90% 18O from 18O2 and occurs at C-3 of arginine leaing to a stereochemistry of the hydroxylated arginine of 2S,3R
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mutant E146A/K147A, predicted to enhance crystallizability, to 2.7 A resolution, space group P43212 with a single protein molecule in the asymmetric unit. The N-terminal domain contains the signature DSBH or beta-barrel that is characteristic of 2OG-dependent oxygenases. The core DSBH is made up of two beta-sheets, one composed of five strands and the second one composed of three strands
to 2.6 A resolution. Comparison with crystal structures of human MYC-induced nuclear antigen MINA53 and nucleolar protein NO66 as well as Rhodothermus marinus YcfD. The observed modes of ribosomal oxygenases hydroxylations have probably evolved into those of other JmjC-containing hydroxylases and the histoneNepsilon-methyl lysine demethylases, both by altering the coordination position from which the ferryl-oxo reacts and by engineering the depth of substrate penetration