2W2I

Crystal structure of the human 2-oxoglutarate oxygenase LOC390245

2W2I の概要

• エントリーDOI: 10.2210/pdb2w2i/pdb
• 分子名称: 2-OXOGLUTARATE OXYGENASE, NICKEL (II) ION, PYRIDINE-2,4-DICARBOXYLIC ACID, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, chromosome 11
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Nucleus : B2RXH2
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 124732.99

構造登録者

Yue, W.W.,Ng, S.,Shafqat, N.,Ugochukwu, E.,McDonough, M.,Pike, A.C.W.,Filippakopoulos, P.,von Delft, F.,Arrowsmith, C.,Weigelt, J.,Edwards, A.,Bountra, C.,Schofield, C.,Oppermann, U. (登録日: 2008-10-31, 公開日: 2009-01-20, 最終更新日: 2023-12-13)

主引用文献

Hillringhaus, L.,Yue, W.W.,Rose, N.R.,Ng, S.S.,Gileadi, C.,Loenarz, C.,Bello, S.H.,Bray, J.E.,Schofield, C.J.,Oppermann, U.
Structural and Evolutionary Basis for the Dual Substrate Selectivity of Human Kdm4 Histone Demethylase Family.
J.Biol.Chem., 286:41616-, 2011

PubMed Abstract: N(ε)-Methylations of histone lysine residues play critical roles in cell biology by "marking" chromatin for transcriptional activation or repression. Lysine demethylases reverse N(ε)-methylation in a sequence- and methylation-selective manner. The determinants of sequence selectivity for histone demethylases have been unclear. The human JMJD2 (KDM4) H3K9 and H3K36 demethylases can be divided into members that act on both H3K9 and H3K36 and H3K9 alone. Kinetic, crystallographic, and mutagenetic studies in vitro and in cells on KDM4A-E reveal that selectivity is determined by multiple interactions within the catalytic domain but outside the active site. Structurally informed phylogenetic analyses reveal that KDM4A-C orthologues exist in all genome-sequenced vertebrates with earlier animals containing only a single KDM4 enzyme. KDM4D orthologues only exist in eutherians (placental mammals) where they are conserved, including proposed substrate sequence-determining residues. The results will be useful for the identification of inhibitors for specific histone demethylases.

PubMed: 21914792
DOI: 10.1074/JBC.M111.283689

実験手法

X-RAY DIFFRACTION (2.1 Å)