2WWU

Crystal structure of the catalytic domain of PHD finger protein 8

Summary for 2WWU

• Entry DOI: 10.2210/pdb2wwu/pdb
• Descriptor: PHD FINGER PROTEIN 8, SULFATE ION, ACETATE ION, ... (6 entities in total)
• Functional Keywords: jmjc domain, epigenetics, metal-binding protein, histone demethylase, metal binding protein
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 44349.71

Authors

Yue, W.W.,Hozjan, V.,Cooper, C.,Tumber, A.,Krojer, T.,Muniz, J.,Allerston, C.,Salah, E.,McDonough, M.A.,von Delft, F.,Arrowsmith, C.,Weigelt, J.,Edwards, A.,Bountra, C.,Schofield, C.J.,Kavanagh, K.L.,Oppermann, U. (deposition date: 2009-10-29, release date: 2009-11-17, Last modification date: 2023-12-20)

Primary citation

Yue, W.W.,Hozjan, V.,Ge, W.,Loenarz, C.,Cooper, C.D.,Schofield, C.J.,Kavanagh, K.L.,Oppermann, U.,McDonough, M.A.
Crystal structure of the PHF8 Jumonji domain, an Nepsilon-methyl lysine demethylase.
FEBS Lett., 584:825-830, 2010

PubMed Abstract: Crystallographic analysis of the catalytic domain of PHD finger protein 8 (PHF8), an N(epsilon)-methyl lysine histone demethylase associated with mental retardation and cleft lip/palate, reveals a double-stranded beta-helix fold with conserved Fe(II) and cosubstrate binding sites typical of the 2-oxoglutarate dependent oxygenases. The PHF8 active site is highly conserved with those of the FBXL10/11demethylases, which are also selective for the di-/mono-methylated lysine states, but differs from that of the JMJD2 demethylases which are selective for tri-/di-methylated states. The results rationalize the lack of activity for the clinically observed F279S PHF8 variant and they will help to identify inhibitors selective for specific N(epsilon)-methyl lysine demethylase subfamilies.

PubMed: 20067792
DOI: 10.1016/j.febslet.2009.12.055

Experimental method

X-RAY DIFFRACTION (2.15 Å)