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. 2019 Dec 30;8:e52983. doi: 10.7554/eLife.52983

Figure 5. The periplasmic multimerization domain.

(A) EccB3 (pink) in the context of the overall ESX-3 dimer (gray transparency). EccB3 has a single-pass transmembrane domain which extends into a large periplasmic domain which was resolved at 5.8 Å resolution. (B) Atomic models of the EccB3 cytoplasmic and transmembrane domains, amino acids 14–93 and 32–93. (C) The N-terminus of EccB3 forms extensive cross-protomer contacts with EccC3 (blue), EccD3-bent (yellow), and EccD3-extended (green). (D) An unsharpened map of the ESX-3 dimer reveals ordered densities consistent with lipids or detergent molecules mediating the interactions between the EccB3 transmembrane helix (marked with a pink dot) and the EccC3 transmembrane helices.

Figure 5.

Figure 5—figure supplement 1. EccB3 maps and models.

Figure 5—figure supplement 1.

(A) Fit between map and model in the linker helix, amino acids 34 to 54. (B) Fit between map and model in the transmembrane helix, amino acids 65 to 85. (C) Fit between homology models of the soluble domain of EccB3 and the periplasmic focused refinement map.