Fig. 3: Organization of the SIN3S complex.
From: Two assembly modes for SIN3 histone deacetylase complexes
a The domain organizations of Pst2, Cph2, and Cph1. b The EM map of the SIN3S complex is shown in three different views. The SIN3S complex contains four modules: Pst2 Lobe (Pst2_HID/HCR, Clr6, and Prw1), two histone binding modules (HB1, consisting of Cph1_NTD and Eaf3; and HB2, consisting of Cph2_NTD and Eaf3’), and scaffold (Pst2_PAH1-3, Cph1_CTD, and Cph2_CTD). c The structure of Pst2 (shown in a cartoon model) in the SIN3S complex (shown in the surface model). d The structure of Cph1 and Cph2. The CTDs of Cph1 and Cph2 form the scaffold with the PAH1/2/3 of Pst2. The NTDs of Cph1 and Cph2 recruit the MRG domains of Eaf3 and Eaf3’ through their SID domains (α2–3), forming the HB1 and HB2 modules, respectively. e The structures of HB1 and HB2 are superposed by the MRG domains. Cph1_PHD is aligned well with the Cph2_PHD1, while the Cph2_PHD2 is away from the BR domain of Cph1.
