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:
Acta crystallographica. Section F, Structural biology communications
影响因子:
--
通讯作者:
Asojo OA
Asojo OA
中科院分区:
其他
文献类型:
--
作者:
Maddy J;Staker BL;Subramanian S;Abendroth J;Edwards TE;Myler PJ;Hybiske K;Asojo OA

文献摘要

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沙眼衣原体是细菌性性传播感染的主要原因。C.沙眼衣原体无机焦磷酸酶(CtPPase)在代谢过程中水解无机焦磷酸盐。CtPPase的2.2μ m分辨率的X射线结构揭示了共同的结构特征,这些结构特征可能有助于将细菌无机焦磷酸酶的抑制剂重新利用为新疗法的起点。 沙眼衣原体是全球细菌性性传播感染的主要原因,也是美国最常报告的感染之一。由于耐药性和目前治疗无法清除持续感染,因此需要开发新的治疗方法。潜在C的结构。沙眼衣原体合理的药物发现目标,包括C。沙眼衣原体无机焦磷酸酶(CtPPase)已经由西雅图传染病结构基因组学中心确定。无机焦磷酸酶在代谢过程中水解无机焦磷酸盐。此外,细菌无机焦磷酸酶已显示出治疗发现的前景。本文报道了CtPPase的2.2 μ m分辨率的X射线结构。 CtPPase的晶体结构揭示了共同的结构特征,这可能有助于将细菌无机焦磷酸酶的抑制剂重新利用为新的C.沙眼
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.