Inhibiting Mycobacterium tuberculosis CoaBC by targeting an allosteric site

The bifunctional enzyme CoaBC catalyses the second and third step in the Coenzyme A (CoA) biosynthesis pathway and is of interest as a M. tuberculosis drug target. Here, the authors present the full-length crystal structure of Mycobacterium smegmatis CoaBC, which is regulated by CoA and CoA thioeste...

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Autores principales:	Vitor Mendes, Simon R. Green, Joanna C. Evans, Jeannine Hess, Michal Blaszczyk, Christina Spry, Owain Bryant, James Cory-Wright, Daniel S-H. Chan, Pedro H. M. Torres, Zhe Wang, Navid Nahiyaan, Sandra O’Neill, Sebastian Damerow, John Post, Tracy Bayliss, Sasha L. Lynch, Anthony G. Coyne, Peter C. Ray, Chris Abell, Kyu Y. Rhee, Helena I. M. Boshoff, Clifton E. Barry, Valerie Mizrahi, Paul G. Wyatt, Tom L. Blundell
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/dfbd7ac1fa2f42d49910fcdc7940c42e
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spelling	oai:doaj.org-article:dfbd7ac1fa2f42d49910fcdc7940c42e2021-12-02T15:07:59ZInhibiting Mycobacterium tuberculosis CoaBC by targeting an allosteric site10.1038/s41467-020-20224-x2041-1723https://doaj.org/article/dfbd7ac1fa2f42d49910fcdc7940c42e2021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20224-xhttps://doaj.org/toc/2041-1723The bifunctional enzyme CoaBC catalyses the second and third step in the Coenzyme A (CoA) biosynthesis pathway and is of interest as a M. tuberculosis drug target. Here, the authors present the full-length crystal structure of Mycobacterium smegmatis CoaBC, which is regulated by CoA and CoA thioesters and forms a dodecamer and by performing a high-throughput screen they identify selective inhibitors of M. tuberculosis CoaB that bind to an allosteric site within CoaB.Vitor MendesSimon R. GreenJoanna C. EvansJeannine HessMichal BlaszczykChristina SpryOwain BryantJames Cory-WrightDaniel S-H. ChanPedro H. M. TorresZhe WangNavid NahiyaanSandra O’NeillSebastian DamerowJohn PostTracy BaylissSasha L. LynchAnthony G. CoynePeter C. RayChris AbellKyu Y. RheeHelena I. M. BoshoffClifton E. BarryValerie MizrahiPaul G. WyattTom L. BlundellNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Vitor Mendes Simon R. Green Joanna C. Evans Jeannine Hess Michal Blaszczyk Christina Spry Owain Bryant James Cory-Wright Daniel S-H. Chan Pedro H. M. Torres Zhe Wang Navid Nahiyaan Sandra O’Neill Sebastian Damerow John Post Tracy Bayliss Sasha L. Lynch Anthony G. Coyne Peter C. Ray Chris Abell Kyu Y. Rhee Helena I. M. Boshoff Clifton E. Barry Valerie Mizrahi Paul G. Wyatt Tom L. Blundell Inhibiting Mycobacterium tuberculosis CoaBC by targeting an allosteric site
description	The bifunctional enzyme CoaBC catalyses the second and third step in the Coenzyme A (CoA) biosynthesis pathway and is of interest as a M. tuberculosis drug target. Here, the authors present the full-length crystal structure of Mycobacterium smegmatis CoaBC, which is regulated by CoA and CoA thioesters and forms a dodecamer and by performing a high-throughput screen they identify selective inhibitors of M. tuberculosis CoaB that bind to an allosteric site within CoaB.
format	article
author	Vitor Mendes Simon R. Green Joanna C. Evans Jeannine Hess Michal Blaszczyk Christina Spry Owain Bryant James Cory-Wright Daniel S-H. Chan Pedro H. M. Torres Zhe Wang Navid Nahiyaan Sandra O’Neill Sebastian Damerow John Post Tracy Bayliss Sasha L. Lynch Anthony G. Coyne Peter C. Ray Chris Abell Kyu Y. Rhee Helena I. M. Boshoff Clifton E. Barry Valerie Mizrahi Paul G. Wyatt Tom L. Blundell
author_facet	Vitor Mendes Simon R. Green Joanna C. Evans Jeannine Hess Michal Blaszczyk Christina Spry Owain Bryant James Cory-Wright Daniel S-H. Chan Pedro H. M. Torres Zhe Wang Navid Nahiyaan Sandra O’Neill Sebastian Damerow John Post Tracy Bayliss Sasha L. Lynch Anthony G. Coyne Peter C. Ray Chris Abell Kyu Y. Rhee Helena I. M. Boshoff Clifton E. Barry Valerie Mizrahi Paul G. Wyatt Tom L. Blundell
author_sort	Vitor Mendes
title	Inhibiting Mycobacterium tuberculosis CoaBC by targeting an allosteric site
title_short	Inhibiting Mycobacterium tuberculosis CoaBC by targeting an allosteric site
title_full	Inhibiting Mycobacterium tuberculosis CoaBC by targeting an allosteric site
title_fullStr	Inhibiting Mycobacterium tuberculosis CoaBC by targeting an allosteric site
title_full_unstemmed	Inhibiting Mycobacterium tuberculosis CoaBC by targeting an allosteric site
title_sort	inhibiting mycobacterium tuberculosis coabc by targeting an allosteric site
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/dfbd7ac1fa2f42d49910fcdc7940c42e
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Inhibiting Mycobacterium tuberculosis CoaBC by targeting an allosteric site

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