Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex

The allosteric regulation of the bienzyme complex imidazole glycerol phosphate synthase (HisFH) remains to be elucidated. Here, the authors provide structural insights into the dynamic allosteric mechanism by which ligand binding to the cyclase and glutaminase active sites of HisFH regulate enzyme a...

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Autores principales:	Jan Philip Wurm, Sihyun Sung, Andrea Christa Kneuttinger, Enrico Hupfeld, Reinhard Sterner, Matthias Wilmanns, Remco Sprangers
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1c1a090281cf40288155ce62446ccc4e
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spelling	oai:doaj.org-article:1c1a090281cf40288155ce62446ccc4e2021-12-02T17:15:21ZMolecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex10.1038/s41467-021-22968-62041-1723https://doaj.org/article/1c1a090281cf40288155ce62446ccc4e2021-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22968-6https://doaj.org/toc/2041-1723The allosteric regulation of the bienzyme complex imidazole glycerol phosphate synthase (HisFH) remains to be elucidated. Here, the authors provide structural insights into the dynamic allosteric mechanism by which ligand binding to the cyclase and glutaminase active sites of HisFH regulate enzyme activation.Jan Philip WurmSihyun SungAndrea Christa KneuttingerEnrico HupfeldReinhard SternerMatthias WilmannsRemco SprangersNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jan Philip Wurm Sihyun Sung Andrea Christa Kneuttinger Enrico Hupfeld Reinhard Sterner Matthias Wilmanns Remco Sprangers Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex
description	The allosteric regulation of the bienzyme complex imidazole glycerol phosphate synthase (HisFH) remains to be elucidated. Here, the authors provide structural insights into the dynamic allosteric mechanism by which ligand binding to the cyclase and glutaminase active sites of HisFH regulate enzyme activation.
format	article
author	Jan Philip Wurm Sihyun Sung Andrea Christa Kneuttinger Enrico Hupfeld Reinhard Sterner Matthias Wilmanns Remco Sprangers
author_facet	Jan Philip Wurm Sihyun Sung Andrea Christa Kneuttinger Enrico Hupfeld Reinhard Sterner Matthias Wilmanns Remco Sprangers
author_sort	Jan Philip Wurm
title	Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex
title_short	Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex
title_full	Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex
title_fullStr	Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex
title_full_unstemmed	Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex
title_sort	molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/1c1a090281cf40288155ce62446ccc4e
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Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex

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