Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6

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 hydroxyl...

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Veröffentlicht in:	Journal of molecular biology 2010-08, Vol.401 (2), p.211-222
Hauptverfasser:	Mantri, Monica, Krojer, Tobias, Bagg, Eleanor A., Webby, Celia J., Butler, Danica S., Kochan, Grazyna, Kavanagh, Kathryn L., Oppermann, Udo, McDonough, Michael A., Schofield, Christopher J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acid Substitution Base Sequence Catalytic Domain Crystallography, X-Ray demethylase DNA Primers - genetics Ehlers–Danlos syndrome type VI histone modification Humans hydroxylase In Vitro Techniques Iron - metabolism Jumonji Domain-Containing Histone Demethylases - chemistry Jumonji Domain-Containing Histone Demethylases - genetics Jumonji Domain-Containing Histone Demethylases - metabolism Ketoglutaric Acids - metabolism lysyl hydroxylase Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Mutant Proteins - chemistry Mutant Proteins - genetics Mutant Proteins - metabolism Nickel - metabolism Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase - chemistry Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase - genetics Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase - metabolism Protein Folding Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Homology, Amino Acid Static Electricity
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