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Figure 1
CtPPase structure. (a) The superposed CtPPase monomers are almost identical, with r.m.s.d.s of ∼0.3 Å for all atoms and ∼0.17 Å for Cα atoms. The monomers are colored from blue (N-terminus) to red (C-terminus). (b) A prototypical family I PPase hexamer was generated from the asymmetric unit trimer (monomers colored green, cyan and magenta) and a symmetry mate (shown in gray). The sodium ion bound in the active site of each monomer is shown as a purple sphere. (c) The CtPPase active-site loop (cyan) is in the open conformation compared with the closed conformation of M. tuberculosis PPase (MtPPase). The pyrophosphate (orange sticks) in the active site is from MtPPase (PDB entry 5kde), while the sodium ion (purple sphere) is from CtPPase (PDB entry 6we5).

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 78| Part 3| March 2022| Pages 135-142
https://doi.org/10.1107/S2053230X22002138
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