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. 2020 Jul 16;295(36):12706–12715. doi: 10.1074/jbc.RA120.012698

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© 2020 Williamson et al.

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Figure 5. — PE5_mt–PPE4_mt interacts with EspG_3mm chaperone in a unique mode compared with ESX-5 PE–PPE dimers. A, structural alignment of the ESX-3 and ESX-5 heterotrimers via the EspG chaperones (36) reveals a difference in the angle of interaction between the PE–PPE heterodimers with their respective chaperone. B, top view of alignment from A. C, superposition of PPE41_mt and PPE4_mt highlights difference in hh loop conformations between ESX-3 (PPE4_mt) and ESX-5 (PPE41_mt). D and E, superposition of PPE alignment from C in context of EspG_3mm interaction (D) and EspG_5mt interaction (E) shows the incompatibility of each PPE protein with noncognate chaperone binding.