6e29 | pdb_00006e29

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

spinqualitylabelsall models 6e29, resolution 1.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6e29 is a 4 chain structure with sequence from Thermothelomyces thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.818Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G2Q1Q9_MYCTT Publication Abstract from PubMed 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-A 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. Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex.,Qu Q, Takahashi YH, Yang Y, Hu H, Zhang Y, Brunzelle JS, Couture JF, Shilatifard A, Skiniotis G Cell. 2018 Aug 23;174(5):1117-1126.e12. doi: 10.1016/j.cell.2018.07.020. Epub, 2018 Aug 9. PMID:30100186 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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