Fig. 1: Cryo-EM structure of Msn5-RanGTP-pPho4.
From: Phosphate-dependent nuclear export via a non-classical NES class recognized by exportin Msn5
a Schematic of Pho4, RanGTP and Msn5. Pho4 has two Pho80-interacting regions (Pho80), a transactivation domain (TA), an IK-NLS, an oligomerization region (oligo) and five Pho85 phosphorylation sites (orange) in its IDR, and a C-terminal basic helix-loop-helix domain (bHLH). Each Msn5 helix is represented by a gray box scaled by its length; h9loop, h15loop and h17-h18loop contain small helices. HEAT repeats are numbered and regions that contact RanGTP or pPho4 are cyan or yellow, respectively. b Immobilized GST-Pho4FL and -Pho41-200, in vitro phosphorylated ( + P) or unphosphorylated (-P), were mixed with Msn5 and excess RanGTP followed by extensive washing. Bound proteins were visualized by Coomassie stained SDS-PAGE. Representative image from triplicate experiment is shown. Source data are provided as a Source Data file. c The final map (left) and two cartoon representations of the Msn5 (gray) -RanGTP (cyan) - pPho41-200 (wheat) structure (center and right). Map features for RanGTP and pPho4 are shown in the center panel, and Msn5 is in rainbow colors with HEAT repeats labeled in the right panel.
