EMD-7335

Single-particle
3.5 Å
EMD-7335 Deposition: 06/01/2018
Map released: 24/01/2018
Last modified: 12/08/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-7335

Cryo-EM structure of PRC2 bound to cofactors AEBP2 and JARID2 in the Extended Active State

EMD-7335

Single-particle
3.5 Å
EMD-7335 Deposition: 06/01/2018
Map released: 24/01/2018
Last modified: 12/08/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: Ternary complex of PRC2 with cofactors AEBP2 and JARID2
Fitted models: 6c24 (Avg. Q-score: 0.433)

Deposition Authors: Kasinath V, Faini M, Poepsel S, Reif D, Feng A, Stjepanovic G, Aebersold R, Nogales E
Structures of human PRC2 with its cofactors AEBP2 and JARID2.
Kasinath V , Faini M , Poepsel S , Reif D , Feng XA , Stjepanovic G , Aebersold R, Nogales E
(2018) Science , 359 , 940 - 944
PUBMED: 29348366
DOI: doi:10.1126/science.aar5700
ISSN: 1095-9203
ASTM: SCIEAS
Abstract:
Transcriptionally repressive histone H3 lysine 27 methylation by Polycomb repressive complex 2 (PRC2) is essential for cellular differentiation and development. Here we report cryo-electron microscopy structures of human PRC2 in a basal state and two distinct active states while in complex with its cofactors JARID2 and AEBP2. Both cofactors mimic the binding of histone H3 tails. JARID2, methylated by PRC2, mimics a methylated H3 tail to stimulate PRC2 activity, whereas AEBP2 interacts with the RBAP48 subunit, mimicking an unmodified H3 tail. SUZ12 interacts with all other subunits within the assembly and thus contributes to the stability of the complex. Our analysis defines the complete architecture of a functionally relevant PRC2 and provides a structural framework to understand its regulation by cofactors, histone tails, and RNA.