Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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.


Journal article


J Mol Biol

Publication Date





211 - 222


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