Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6.
|Abstract||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 o ... [truncated at 450 characters in length]|
|Author||Mantri, Monica; Krojer, Tobias; Bagg, Eleanor A; et al|
|Subject||Amino Acid Sequence Amino Acid Substitution Base Sequence Catalytic Domain Crystallography, X-Ray DNA Primers Humans 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 genetics metabolism chemistry genetics metabolism metabolism chemistry genetics metabolism metabolism chemistry genetics metabolism chemistry genetics metabolism|