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. Author manuscript; available in PMC: 2009 Nov 28.
Published in final edited form as: Science. 2008 Oct 30;322(5906):1369–1373. doi: 10.1126/science.1165886

Fig. 4. Architecture of ACE1.

Fig. 4

(A) ACE1 containing proteins are shown as cylinders and sheets. Crowns are shown in blue, trunks in orange, tails in green, and other domains in gray. Modules with predicted structures are shown half-transparent. (PDB codes: 2QX5, Nic96; 3BG1, Nup145C; 3CQC, Nup107 (Nup84 homolog); 2PM6, Sec31) (B) Cartoon illustrating the similarity and modular nature of the ACE1 element. The N-terminal elaborations are for Nic96 a coiled-coil domain that interacts with the Nsp1 complex, for Nup85 the Seh1-interacting insertion blade, for Nup145C the Sec13-interacting insertion blade preceded by an autocatalytic cleavage domain and Nup145N, and for Sec31 the Sec13-interacting insertion blade is preceded by its own N-terminal 7-bladed β-propeller. Sec31 has a unique proline rich insertion C-terminal to its trunk module followed by a conserved region predicted to be α-helical.