Structural highlights
FunctionIPYR_CHLTR Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. Publication Abstract from PubMedChlamydia trachomatis is the leading cause of bacterial sexually transmitted infections globally and is one of the most commonly reported infections in the United States. There is a need to develop new therapeutics due to drug resistance and the failure of current treatments to clear persistent infections. Structures of potential C. trachomatis rational drug-discovery targets, including C. trachomatis inorganic pyrophosphatase (CtPPase), have been determined by the Seattle Structural Genomics Center for Infectious Disease. Inorganic pyrophosphatase hydrolyzes inorganic pyrophosphate during metabolism. Furthermore, bacterial inorganic pyrophosphatases have shown promise for therapeutic discovery. Here, a 2.2 A resolution X-ray structure of CtPPase is reported. The crystal structure of CtPPase reveals shared structural features that may facilitate the repurposing of inhibitors identified for bacterial inorganic pyrophosphatases as starting points for new therapeutics for C. trachomatis. Crystal structure of an inorganic pyrophosphatase from Chlamydia trachomatis D/UW-3/Cx.,Maddy J, Staker BL, Subramanian S, Abendroth J, Edwards TE, Myler PJ, Hybiske K, Asojo OA Acta Crystallogr F Struct Biol Commun. 2022 Mar 1;78(Pt 3):135-142. doi:, 10.1107/S2053230X22002138. Epub 2022 Feb 28. PMID:35234139[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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