Overall structure of the human CPSF160–WDR33–CPSF30–AUUAAA PAS RNA quaternary complex. (A) Domain organizations of human CPSF160, WDR33, and CPSF30. The domains of CPSF160 and WDR33 are labeled, and the zinc fingers of CPSF30 are in green. The collagen-like segment of WDR33 is in gray. The canonical isoform of CPSF30 is shown. Isoform 2 studied here lacks residues 191–215. (B) Binding mode of the AAUAAA RNA by mPSF (Sun et al. 2018). Hydrogen-bonding interactions are shown as dashed lines (red), and the side chains of amino acid residues involved are omitted for clarity. (C) Local resolution map for the quaternary complex. (D) Overall structure of the quaternary complex, colored as in A. The PAS RNA is in orange. The structure of the AAUAAA quaternary complex is shown in gray. The superposition is based on WDR33, and the difference in position of CPSF160 BPB is readily visible. (E) Overall structure of the quaternary complex, viewed after a rotation of 90° around the vertical axis. Panel C was produced with Chimera (Pettersen et al. 2004), and the other structure figures were produced with PyMOL (www.pymol.org), unless noted otherwise.
