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6WE5

Crystal structure of an inorganic pyrophosphatase from Chlamydia trachomatis D/UW-3/Cx

Summary for 6WE5
Entry DOI10.2210/pdb6we5/pdb
DescriptorInorganic pyrophosphatase, SODIUM ION (3 entities in total)
Functional Keywordsnational institute of allergy and infectious diseases, niaid, structural genomics, sexually transmitted infections, sti, std, pyrophosphate phospho-hydrolase, seattle structural genomics center for infectious disease, ssgcid, hydrolase
Biological sourceChlamydia trachomatis (strain D/UW-3/Cx)
Total number of polymer chains3
Total formula weight73409.65
Authors
Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2020-04-01, release date: 2020-04-08, Last modification date: 2023-10-18)
Primary citationMaddy, J.,Staker, B.L.,Subramanian, S.,Abendroth, J.,Edwards, T.E.,Myler, P.J.,Hybiske, K.,Asojo, O.A.
Crystal structure of an inorganic pyrophosphatase from Chlamydia trachomatis D/UW-3/Cx.
Acta Crystallogr.,Sect.F, 78:135-142, 2022
Cited by
PubMed Abstract: 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.
PubMed: 35234139
DOI: 10.1107/S2053230X22002138
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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