2YBA

Crystal structure of Nurf55 in complex with histone H3

Summary for 2YBA

• Entry DOI: 10.2210/pdb2yba/pdb
• Related: 1KNA 1KNE 2XYI 2YB8
• Descriptor: PROBABLE HISTONE-BINDING PROTEIN CAF1, HISTONE H3 (3 entities in total)
• Functional Keywords: transcription, rbbp4, rbbp7, rbap46, rbap48, polycomb, prc2, wd40 domain, histone methylation h3k27, h3k4, chromatin remodelling
• Biological source: DROSOPHILA MELANOGASTER (FRUIT FLY); More
• Total number of polymer chains: 4
• Total formula weight: 99678.09

Authors

Schmitges, F.W.,Prusty, A.B.,Faty, M.,Stutzer, A.,Lingaraju, G.M.,Aiwazian, J.,Sack, R.,Hess, D.,Li, L.,Zhou, S.,Bunker, R.D.,Wirth, U.,Bouwmeester, T.,Bauer, A.,Ly-Hartig, N.,Zhao, K.,Chan, H.,Gu, J.,Gut, H.,Fischle, W.,Muller, J.,Thoma, N.H. (deposition date: 2011-03-02, release date: 2011-05-11, Last modification date: 2024-05-01)

Primary citation

Schmitges, F.W.,Prusty, A.B.,Faty, M.,Stutzer, A.,Lingaraju, G.M.,Aiwazian, J.,Sack, R.,Hess, D.,Li, L.,Zhou, S.,Bunker, R.D.,Wirth, U.,Bouwmeester, T.,Bauer, A.,Ly-Hartig, N.,Zhao, K.,Chan, H.,Gu, J.,Gut, H.,Fischle, W.,Muller, J.,Thoma, N.H.
Histone Methylation by Prc2 is Inhibited by Active Chromatin Marks
Mol.Cell, 42:330-, 2011

PubMed Abstract: The Polycomb repressive complex 2 (PRC2) confers transcriptional repression through histone H3 lysine 27 trimethylation (H3K27me3). Here, we examined how PRC2 is modulated by histone modifications associated with transcriptionally active chromatin. We provide the molecular basis of histone H3 N terminus recognition by the PRC2 Nurf55-Su(z)12 submodule. Binding of H3 is lost if lysine 4 in H3 is trimethylated. We find that H3K4me3 inhibits PRC2 activity in an allosteric fashion assisted by the Su(z)12 C terminus. In addition to H3K4me3, PRC2 is inhibited by H3K36me2/3 (i.e., both H3K36me2 and H3K36me3). Direct PRC2 inhibition by H3K4me3 and H3K36me2/3 active marks is conserved in humans, mouse, and fly, rendering transcriptionally active chromatin refractory to PRC2 H3K27 trimethylation. While inhibition is present in plant PRC2, it can be modulated through exchange of the Su(z)12 subunit. Inhibition by active chromatin marks, coupled to stimulation by transcriptionally repressive H3K27me3, enables PRC2 to autonomously template repressive H3K27me3 without overwriting active chromatin domains.

PubMed: 21549310
DOI: 10.1016/J.MOLCEL.2011.03.025

Experimental method

X-RAY DIFFRACTION (2.55 Å)