3K2O

Structure of an oxygenase

3K2O の概要

• エントリーDOI: 10.2210/pdb3k2o/pdb
• 分子名称: Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6, NICKEL (II) ION, SODIUM ION, ... (8 entities in total)
• 機能のキーワード: structural genomics consortium, sgc, chromatin regulator, developmental protein, differentiation, dioxygenase, iron, metal-binding, mrna processing, mrna splicing, nucleus, oxidoreductase, transcription, transcription regulation
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus, nucleoplasm: Q6NYC1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80666.06

構造登録者

Krojer, T.,McDonough, M.A.,Clifton, I.J.,Mantri, M.,Ng, S.S.,Pike, A.C.W.,Butler, D.S.,Webby, C.J.,Kochan, G.,Bhatia, C.,Bray, J.E.,Chaikuad, A.,Gileadi, O.,von Delft, F.,Weigelt, J.,Arrowsmith, C.H.,Bountra, C.,Edwards, A.M.,Schofield, C.J.,Kavanagh, K.L.,Oppermann, U.,Structural Genomics Consortium (SGC) (登録日: 2009-09-30, 公開日: 2009-11-03, 最終更新日: 2024-11-13)

主引用文献

Mantri, M.,Krojer, T.,Bagg, E.A.,Webby, C.A.,Butler, D.S.,Kochan, G.,Kavanagh, K.L.,Oppermann, U.,McDonough, M.A.,Schofield, C.J.
Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6.
J.Mol.Biol., 401:211-222, 2010

PubMed 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 N(varepsilon)-demethylation, as for analogous enzymes.

PubMed: 20685276
DOI: 10.1016/j.jmb.2010.05.054

実験手法

X-RAY DIFFRACTION (1.75 Å)