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. 2020 Jan 29;6(5):eaax8286. doi: 10.1126/sciadv.aax8286

Fig. 2. The P2 domain β hairpin is responsible for membrane binding.

Fig. 2

(A and B) Atomic structure of P2 domain showing pseudo-threefold symmetry repeat colored blue, pink, and green. Disulfide bonds linking the β strands are labeled in yellow; the β-hairpin region is marked with a dashed rectangular box. (C) Superimposition of the P2 cryo-EM structure (pre-pore model in green and pore model in purple) and 10 crystallographically distinct copies of the P2 domain (gray). (D and E) Ultracentrifugation-based liposome-binding assays of mPFN2 P2 domain; the liposomes contained different concentrations of phosphatidylserine (PS) (D) or negatively charged or neutral lipids (E). PC, phosphatidylcholine; PE, phosphatidylethanolamine; CL, cardiolipin; SM, sphingomyelin; 30E, 30% of E. coli total lipid extract; 40E, 40% of E. coli total lipid extract; LPSS, LPS from S. enterica; LPSE, LPS from E. coli. (F) Ultracentrifugation-based liposome-binding assays of mPFN2 P2 domain and P2Δhairpin truncation mutant. Green underlines in (E) and (F) indicate the same liposome composition with 50% PC/10% PS/40% E. coli total lipid extract. WT, wild type.