Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release

Mutation of the C-terminal extension of 5′-aminolevulinate synthase 2 (ALAS2) is the molecular cause for X-linked protoporphyria, but the underlying mechanism is unclear. Based on crystal structures and MD simulations of ALAS2, the authors here show how the C-terminal extension regulates ALAS2 activ...

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Autores principales:	Henry J. Bailey, Gustavo A. Bezerra, Jason R. Marcero, Siladitya Padhi, William R. Foster, Elzbieta Rembeza, Arijit Roy, David F. Bishop, Robert J. Desnick, Gopalakrishnan Bulusu, Harry A. Dailey, Wyatt W. Yue
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b469b0462bc94b0e8a1d29a9113fb32b
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spelling	oai:doaj.org-article:b469b0462bc94b0e8a1d29a9113fb32b2021-12-02T15:03:12ZHuman aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release10.1038/s41467-020-16586-x2041-1723https://doaj.org/article/b469b0462bc94b0e8a1d29a9113fb32b2020-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16586-xhttps://doaj.org/toc/2041-1723Mutation of the C-terminal extension of 5′-aminolevulinate synthase 2 (ALAS2) is the molecular cause for X-linked protoporphyria, but the underlying mechanism is unclear. Based on crystal structures and MD simulations of ALAS2, the authors here show how the C-terminal extension regulates ALAS2 activity.Henry J. BaileyGustavo A. BezerraJason R. MarceroSiladitya PadhiWilliam R. FosterElzbieta RembezaArijit RoyDavid F. BishopRobert J. DesnickGopalakrishnan BulusuHarry A. DaileyWyatt W. YueNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Henry J. Bailey Gustavo A. Bezerra Jason R. Marcero Siladitya Padhi William R. Foster Elzbieta Rembeza Arijit Roy David F. Bishop Robert J. Desnick Gopalakrishnan Bulusu Harry A. Dailey Wyatt W. Yue Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release
description	Mutation of the C-terminal extension of 5′-aminolevulinate synthase 2 (ALAS2) is the molecular cause for X-linked protoporphyria, but the underlying mechanism is unclear. Based on crystal structures and MD simulations of ALAS2, the authors here show how the C-terminal extension regulates ALAS2 activity.
format	article
author	Henry J. Bailey Gustavo A. Bezerra Jason R. Marcero Siladitya Padhi William R. Foster Elzbieta Rembeza Arijit Roy David F. Bishop Robert J. Desnick Gopalakrishnan Bulusu Harry A. Dailey Wyatt W. Yue
author_facet	Henry J. Bailey Gustavo A. Bezerra Jason R. Marcero Siladitya Padhi William R. Foster Elzbieta Rembeza Arijit Roy David F. Bishop Robert J. Desnick Gopalakrishnan Bulusu Harry A. Dailey Wyatt W. Yue
author_sort	Henry J. Bailey
title	Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release
title_short	Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release
title_full	Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release
title_fullStr	Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release
title_full_unstemmed	Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release
title_sort	human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/b469b0462bc94b0e8a1d29a9113fb32b
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Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release

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