Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2

Isocitrate lyase (ICL) isoforms 1 and 2 are enzymes in the glyoxylate and methylcitrate cycles that enable Mycobacterium tuberculosis (Mtb) to use lipids as a carbon source. Here the authors present the ligand-free Mtb ICL2 and acetyl-CoA bound ICL2 crystal structures, which reveal a structural reor...

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Autores principales:	Ram Prasad Bhusal, Wanting Jiao, Brooke X. C. Kwai, Jóhannes Reynisson, Annabelle J. Collins, Jonathan Sperry, Ghader Bashiri, Ivanhoe K. H. Leung
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/84f707b24cca4ccd924cf9d174e6fea6
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spelling	oai:doaj.org-article:84f707b24cca4ccd924cf9d174e6fea62021-12-02T16:57:42ZAcetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 210.1038/s41467-019-12614-72041-1723https://doaj.org/article/84f707b24cca4ccd924cf9d174e6fea62019-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12614-7https://doaj.org/toc/2041-1723Isocitrate lyase (ICL) isoforms 1 and 2 are enzymes in the glyoxylate and methylcitrate cycles that enable Mycobacterium tuberculosis (Mtb) to use lipids as a carbon source. Here the authors present the ligand-free Mtb ICL2 and acetyl-CoA bound ICL2 crystal structures, which reveal a structural reorganisation upon acetyl-CoA binding that leads to an activation of its isocitrate lyase and methylcitrate lyase activities.Ram Prasad BhusalWanting JiaoBrooke X. C. KwaiJóhannes ReynissonAnnabelle J. CollinsJonathan SperryGhader BashiriIvanhoe K. H. LeungNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-7 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ram Prasad Bhusal Wanting Jiao Brooke X. C. Kwai Jóhannes Reynisson Annabelle J. Collins Jonathan Sperry Ghader Bashiri Ivanhoe K. H. Leung Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2
description	Isocitrate lyase (ICL) isoforms 1 and 2 are enzymes in the glyoxylate and methylcitrate cycles that enable Mycobacterium tuberculosis (Mtb) to use lipids as a carbon source. Here the authors present the ligand-free Mtb ICL2 and acetyl-CoA bound ICL2 crystal structures, which reveal a structural reorganisation upon acetyl-CoA binding that leads to an activation of its isocitrate lyase and methylcitrate lyase activities.
format	article
author	Ram Prasad Bhusal Wanting Jiao Brooke X. C. Kwai Jóhannes Reynisson Annabelle J. Collins Jonathan Sperry Ghader Bashiri Ivanhoe K. H. Leung
author_facet	Ram Prasad Bhusal Wanting Jiao Brooke X. C. Kwai Jóhannes Reynisson Annabelle J. Collins Jonathan Sperry Ghader Bashiri Ivanhoe K. H. Leung
author_sort	Ram Prasad Bhusal
title	Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2
title_short	Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2
title_full	Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2
title_fullStr	Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2
title_full_unstemmed	Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2
title_sort	acetyl-coa-mediated activation of mycobacterium tuberculosis isocitrate lyase 2
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/84f707b24cca4ccd924cf9d174e6fea6
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Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2

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