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 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_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Mantri M,Krojer T,Bagg EA,Webby CJ,Butler DS,Kochan G,Kavanagh KL,Oppermann U,McDonough MA,Schofield CJsubject
Has Abstractpub_date
2010-08-13 00:00:00pages
211-22issue
2eissn
0022-2836issn
1089-8638pii
S0022-2836(10)00558-9journal_volume
401pub_type
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