Fig. 1: Cryo-EM structure of the RalGAP complex.
From: Structure and mechanism of the RalGAP tumor suppressor complex
a Domain architecture of RGα2 and RGβ. HEAT: α-solenoid HEAT repeat-like domain; SD split stabilization and dimerization domain; H hug domain; (p)GAP (pseudo-) GTPase activating protein domain. b Negative stain image of a full RalGAP particle in comparison to the 3D reconstruction of the half-particle. The red arrow marks the connection between two heterodimeric half-particles. c Composite experimental map of RalGAP (half)-particles. d Model of the RGα2/RGβ heterodimer and the N-terminal portion of a second RGβ subunit. Domains are colored as in 1 A. Dashed lines indicate the interface of both half-particles. e Close-up of the SD domain heterodimerization interface. The β-strands (1–5) and α-helices (A–D) of the SD domains are labeled. f Interaction of the RGα2 hug domain with RGβ. g Interaction of the RGβ hug domain with RGα2.
