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Figure 4
The bacterial PPase allosteric binding site. The putative allosteric binding site of CtPPase identified from superposition of CtPPase (PDB entry 6we5) with MtPPase (PDB entries 5kde and 5kdf) and BpPPase (PDB entries 3ej0 and 3ej2). (a) Coil diagram of CtPPase (red and white) superimposed on the MtPPase structures with allosteric inhibitors (PDB entries 5kde, yellow, and 5kdf, magenta) and BpPPase bound with fragment compounds (PDB entries 3ej0, wheat, and 3ej2, blue). The location of the compounds is indicated with a black oval. The circumference of the coil represents the relative structural conservation compared with 41 other PPase structures (the same structures as indicated in Fig. 2[link]). (b) A solvent-accessible surface diagram of CtPPase calculated with ENDscript reveals a potential binding pocket labeled the allosteric site on the CtPPase surface in proximity to the compounds.

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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