6E29

Crystal structure of Myceliophteria_thermophila Cps50 (Swd1) beta-propeller domain

Summary for 6E29

• Entry DOI: 10.2210/pdb6e29/pdb
• Descriptor: SWD1-like protein (2 entities in total)
• Functional Keywords: histone, epigenetics, compass, histone h3 lys-4 methylation, mll1, set1, protein binding
• Biological source: Myceliophthora thermophila (Sporotrichum thermophile)
• Total number of polymer chains: 4
• Total formula weight: 156445.38

Authors

Joshi, M.,Yang, Y.,Brunzelle, J.S.,Couture, J.F. (deposition date: 2018-07-10, release date: 2018-07-25, Last modification date: 2023-10-11)

Primary citation

Qu, Q.,Takahashi, Y.H.,Yang, Y.,Hu, H.,Zhang, Y.,Brunzelle, J.S.,Couture, J.F.,Shilatifard, A.,Skiniotis, G.
Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex.
Cell, 174:1117-, 2018

PubMed Abstract: The methylation of histone 3 lysine 4 (H3K4) is carried out by an evolutionarily conserved family of methyltransferases referred to as complex of proteins associated with Set1 (COMPASS). The activity of the catalytic SET domain (su(var)3-9, enhancer-of-zeste, and trithorax) is endowed through forming a complex with a set of core proteins that are widely shared from yeast to humans. We obtained cryo-electron microscopy (cryo-EM) maps of the yeast Set1/COMPASS core complex at overall 4.0- to 4.4-Å resolution, providing insights into its structural organization and conformational dynamics. The Cps50 C-terminal tail weaves within the complex to provide a central scaffold for assembly. The SET domain, snugly positioned at the junction of the Y-shaped complex, is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3). The mobile SET-I motif of the SET domain is engaged by Cps30, explaining its key role in COMPASS catalytic activity toward higher H3K4 methylation states.

PubMed: 30100186
DOI: 10.1016/j.cell.2018.07.020

Experimental method

X-RAY DIFFRACTION (1.818 Å)