Crystal structure of an inorganic pyrophosphatase from Chlamydia trachomatis D/UW-3/Cx.
Crystal structure of an inorganic pyrophosphatase from Chlamydia trachomatis D/UW-3/Cx.
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来自沙眼衣原体D/UW-3/CX的无机焦磷酸酶的晶体结构。
DOI:
10.1107/s2053230x22002138
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发表时间:
2022-03-01
期刊:
影响因子:
--
通讯作者:
Asojo OA
中科院分区:
文献类型:
--
作者:
Maddy J;Staker BL;Subramanian S;Abendroth J;Edwards TE;Myler PJ;Hybiske K;Asojo OA
Chlamydia trachomatis is the leading cause of bacterial sexually transmitted infections. C. trachomatis inorganic pyrophosphatase (CtPPase) hydrolyzes inorganic pyrophosphate during metabolism. A 2.2 Å resolution X-ray 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. Chlamydia 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 Å 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.