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

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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Detalles Bibliográficos
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
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Science
Q
Acceso en línea:https://doaj.org/article/b469b0462bc94b0e8a1d29a9113fb32b
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Sumario: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.

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