Crystal structure of the 2-Oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6

Mantri, Monica, Krojer, Tobias, Bagg, Eleanor A., Webby, Celia J., Butler, Danica S., Kochan, Grazyna, Kavanagh, Kathryn L., Oppermann, Udo, McDonough, Michael A. and Schofield, Christopher J. (2010) Crystal structure of the 2-Oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6. Journal of Molecular Biology, 401 2: 211-222. doi:10.1016/j.jmb.2010.05.054

Author 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.
Title Crystal structure of the 2-Oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6
Journal name Journal of Molecular Biology   Check publisher's open access policy
ISSN 0022-2836
Publication date 2010-08-13
Sub-type Article (original research)
DOI 10.1016/j.jmb.2010.05.054
Open Access Status Not Open Access
Volume 401
Issue 2
Start page 211
End page 222
Total pages 12
Place of publication London, United Kingdom
Publisher Academic Press
Language eng
Formatted 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 Nɛ-demethylation, as for analogous enzymes.
Keyword Demethylase
Histone modification
Ehlers–Danlos syndrome type VI
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Faculty of Health and Behavioural Sciences -- Publications
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Created: Sun, 30 Oct 2011, 20:01:16 EST by Celia Webby on behalf of Faculty Of Health Sciences