5WAK

Crystal Structure of a Suz12-Rbbp4 Binary Complex

Summary for 5WAK

• Entry DOI: 10.2210/pdb5wak/pdb
• Descriptor: Histone-binding protein RBBP4, Polycomb protein SUZ12, ZINC ION (3 entities in total)
• Functional Keywords: methyltransferase, transcription
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus: Q09028 Q15022
• Total number of polymer chains: 2
• Total formula weight: 105119.03

Authors

Chen, S.,Jiao, L.,Liu, X. (deposition date: 2017-06-26, release date: 2018-03-14, Last modification date: 2023-10-04)

Primary citation

Chen, S.,Jiao, L.,Shubbar, M.,Yang, X.,Liu, X.
Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding.
Mol. Cell, 69:840-852.e5, 2018

PubMed Abstract: Developmentally regulated accessory subunits dictate PRC2 function. Here, we report the crystal structures of a 120 kDa heterotetrameric complex consisting of Suz12, Rbbp4, Jarid2, and Aebp2 fragments that is minimally active in nucleosome binding and of an inactive binary complex of Suz12 and Rbbp4. Suz12 contains two unique structural platforms that define distinct classes of PRC2 holo complexes for chromatin binding. Aebp2 and Phf19 compete for binding of a non-canonical C2 domain of Suz12; Jarid2 and EPOP occupy an overlapped Suz12 surface required for chromatin association of PRC2. Suz12 and Aebp2 progressively block histone H3K4 binding to Rbbp4, suggesting that Rbbp4 may not be directly involved in PRC2 inhibition by the active H3K4me3 histone mark. Nucleosome binding enabled by Jarid2 and Aebp2 is in part accounted for by the structures, which also reveal that disruption of the Jarid2-Suz12 interaction may underlie the disease mechanism of an oncogenic chromosomal translocation of Suz12.

PubMed: 29499137
DOI: 10.1016/j.molcel.2018.01.039

Experimental method

X-RAY DIFFRACTION (3.2 Å)