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Lysyl and prolyl hydroxylations are well-known post-translational modifications to animal and plant proteins with extracellular roles. More recent work has indicated that the hydroxylation of intracellular animal proteins may be common. JMJD6 catalyses the iron- and 2-oxoglutarate-dependent hydroxylation of lysyl residues in arginine-serine-rich domains of RNA splicing-related proteins. We report crystallographic studies on the catalytic domain of JMJD6 in complex with Ni(II) substituting for Fe(II). Together with mutational studies, the structural data suggest how JMJD6 binds its lysyl residues such that it can catalyse C-5 hydroxylation rather than Nepsilon-demethylation, as for analogous enzymes.

Original publication




Journal article


Journal of molecular biology

Publication Date





211 - 222


Department of Chemistry and Oxford Centre for Integrative Systems Biology, Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, UK.


Humans, Iron, Nickel, Ketoglutaric Acids, Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase, Recombinant Proteins, DNA Primers, Crystallography, X-Ray, Amino Acid Substitution, Mutagenesis, Site-Directed, Amino Acid Sequence, Catalytic Domain, Base Sequence, Protein Folding, Sequence Homology, Amino Acid, Models, Molecular, Molecular Sequence Data, Mutant Proteins, Static Electricity, Jumonji Domain-Containing Histone Demethylases, In Vitro Techniques