5m5g

Crystal structure of the Chaetomium Thermophilum polycomb repressive complex 2 (PRC2)

spinqualitylabelsall models 5m5g, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5m5g is a 4 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.27Å Ligands: M3L, SAH, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SUZ12_CHATD Component of the of the Polycomb Repressive Complex 2 (PRC2), a histone H3 lysine methyltransferase responsible for generating mono-, di-, and tri-methylation on Lys27 (H3K27me1, H3K27me2 and H3K27me3) (PubMed:26472914, PubMed:28008037). The tri-methylated form is known to be critical in gene repression, and its proper placement is essential in defining repression patterns during development (PubMed:26472914, PubMed:28008037). SUZ12 is not a catalytic subunit but is required for the complex regulation of histone H3 lysine methylation by EZH2 (PubMed:26472914). Publication Abstract from PubMed Jiao and Liu (Research Articles, 16 October 2015, aac4383) reported the crystal structure of the protein complex polycomb repressive complex 2 from Chaetomium thermophilum This landmark structure has brought invaluable insights into the activation mechanism of this essential methyltransferase. However, the analysis of the x-ray data discussed below suggests that the description of oncogenic H3K27M peptide binding to the active site is incorrect. Comment on "Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2".,Zhang Y, Justin N, Wilson JR, Gamblin SJ Science. 2016 Dec 23;354(6319):1543. doi: 10.1126/science.aaf6236. PMID:28008037 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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