- PDB-8gcc: T. cruzi topoisomerase II alpha bound to dsDNA and the covalent i... -
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Basic information
Entry
Database: PDB / ID: 8gcc
Title
T. cruzi topoisomerase II alpha bound to dsDNA and the covalent inhibitor CT1
Components
DNA (28-MER)
DNA topoisomerase 2
Keywords
ISOMERASE / Topoisomerase / DNA binding protein / Topoisomerase inhibitor
Function / homology
Function and homology information
DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity / DNA topoisomerase (ATP-hydrolysing) / DNA topological change / DNA binding / ATP binding / metal ion binding Similarity search - Function
DNA topoisomerase 2, TOPRIM domain / DNA topoisomerase II, eukaryotic-type / C-terminal associated domain of TOPRIM / C-terminal associated domain of TOPRIM / DNA topoisomerase, type IIA, alpha-helical domain superfamily / DNA topoisomerase, type IIA, domain A / DNA topoisomerase, type IIA, domain A, alpha-beta / DNA gyrase/topoisomerase IV, subunit A / DNA Topoisomerase IV / DNA topoisomerase, type IIA, subunit B, domain 2 ...DNA topoisomerase 2, TOPRIM domain / DNA topoisomerase II, eukaryotic-type / C-terminal associated domain of TOPRIM / C-terminal associated domain of TOPRIM / DNA topoisomerase, type IIA, alpha-helical domain superfamily / DNA topoisomerase, type IIA, domain A / DNA topoisomerase, type IIA, domain A, alpha-beta / DNA gyrase/topoisomerase IV, subunit A / DNA Topoisomerase IV / DNA topoisomerase, type IIA, subunit B, domain 2 / DNA gyrase B / DNA topoisomerase, type IIA / DNA topoisomerase, type IIA, conserved site / DNA topoisomerase II signature. / TopoisomeraseII / DNA topoisomerase, type IIA, subunit B, C-terminal / DNA topoisomerase, type IIA-like domain superfamily / Toprim domain profile. / TOPRIM domain / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold Similarity search - Domain/homology
Journal: Science / Year: 2023 Title: Cyanotriazoles are selective topoisomerase II poisons that rapidly cure trypanosome infections. Authors: Srinivasa P S Rao / Matthew K Gould / Jonas Noeske / Manuel Saldivia / Rajiv S Jumani / Pearly S Ng / Olivier René / Yen-Liang Chen / Marcel Kaiser / Ryan Ritchie / Amanda Fortes Francisco ...Authors: Srinivasa P S Rao / Matthew K Gould / Jonas Noeske / Manuel Saldivia / Rajiv S Jumani / Pearly S Ng / Olivier René / Yen-Liang Chen / Marcel Kaiser / Ryan Ritchie / Amanda Fortes Francisco / Nila Johnson / Debjani Patra / Harry Cheung / Colin Deniston / Andreas D Schenk / Wilian A Cortopassi / Remo S Schmidt / Natalie Wiedemar / Bryanna Thomas / Rima Palkar / Nahdiyah A Ghafar / Vanessa Manoharan / Catherine Luu / Jonathan E Gable / Kah Fei Wan / Elmarie Myburgh / Jeremy C Mottram / Whitney Barnes / John Walker / Charles Wartchow / Natasha Aziz / Colin Osborne / Juergen Wagner / Christopher Sarko / John M Kelly / Ujjini H Manjunatha / Pascal Mäser / Jan Jiricek / Suresh B Lakshminarayana / Michael P Barrett / Thierry T Diagana / Abstract: Millions who live in Latin America and sub-Saharan Africa are at risk of trypanosomatid infections, which cause Chagas disease and human African trypanosomiasis (HAT). Improved HAT treatments are ...Millions who live in Latin America and sub-Saharan Africa are at risk of trypanosomatid infections, which cause Chagas disease and human African trypanosomiasis (HAT). Improved HAT treatments are available, but Chagas disease therapies rely on two nitroheterocycles, which suffer from lengthy drug regimens and safety concerns that cause frequent treatment discontinuation. We performed phenotypic screening against trypanosomes and identified a class of cyanotriazoles (CTs) with potent trypanocidal activity both in vitro and in mouse models of Chagas disease and HAT. Cryo-electron microscopy approaches confirmed that CT compounds acted through selective, irreversible inhibition of trypanosomal topoisomerase II by stabilizing double-stranded DNA:enzyme cleavage complexes. These findings suggest a potential approach toward successful therapeutics for the treatment of Chagas disease.
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