Extended Data Fig. 4: Structural features of DmSERINC.
From: A bipartite structural organization defines the SERINC family of HIV-1 restriction factors
a, Transmembrane topology diagram of DmSERINC structure, with residues not resolved in the cryo-EM map shaded in gray. b, Topology diagram of the SERINC protein fold, colored as in Fig. 1b. ECLs and ICLs are labeled, with disulfide bonds and subdomains A and B. c, Scatter plot of top 500 results from an analysis using Dali server, showing numbers of aligned residues versus r.m.s. deviations (Å) of Cα atom positions. d, DmSERINC hexamer colored by conservation; Guillemet indicates the viewpoint on the protomer-protomer interface labeled with an asterisk that is shown in the side view on the right. e, Examples of DmSERINC cryo-EM map with fitted model. f, Two disulfide bonds identified on the extracellular side of DmSERINC. Left, Cryo-EM map showing profile of the Cys71-Cys91 disulfide bond within ECL1. Right, Cryo-EM map showing profile of the Cys238-Cys299 disulfide bond between ECL3 and ECL4. g−i, Thermostability of the DmSERINC hexamer (g), monomer (h), and SERINC5 (i) with the addition of reducing agents (0.5 mM DTT and 0.5 mM TCEP); data shown are mean and s.d. n = 3 or 4 technical replicates. Data are provided in Source Data. j, Molecular dynamic simulations of solvation. Top left, Density analysis of waters (blue surface) around DmSERINC (gray cartoon) in one repeat of an atomistic 230-ns simulation. Bottom left, Water density shown as a 2D heat map slice. Right, DmSERINC residues implicated in controlling water wire highlighted in green.
