3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme

Lázaro et. al. report the first 3D structure of a large glutamate dehydrogenase (L-GDH), the one corresponding to the Mycobacterium smegmatis enzyme composed of 180 kDa subunits (mL-GDH180), obtained by X-ray crystallography and cryo-electron microscopy. This structure reveals that mL-GDH180 assembl...

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Autores principales:	Melisa Lázaro, Roberto Melero, Charlotte Huet, Jorge P. López-Alonso, Sandra Delgado, Alexandra Dodu, Eduardo M. Bruch, Luciano A. Abriata, Pedro M. Alzari, Mikel Valle, María-Natalia Lisa
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/ee3d06ba507e400089d1f6209e598b96
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spelling	oai:doaj.org-article:ee3d06ba507e400089d1f6209e598b962021-12-02T18:25:02Z3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme10.1038/s42003-021-02222-x2399-3642https://doaj.org/article/ee3d06ba507e400089d1f6209e598b962021-06-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02222-xhttps://doaj.org/toc/2399-3642Lázaro et. al. report the first 3D structure of a large glutamate dehydrogenase (L-GDH), the one corresponding to the Mycobacterium smegmatis enzyme composed of 180 kDa subunits (mL-GDH180), obtained by X-ray crystallography and cryo-electron microscopy. This structure reveals that mL-GDH180 assembles as tetramers with the N- and C-terminal domains being involved in inter-subunit contacts and unveils unique features of the subfamily of L-GDHs.Melisa LázaroRoberto MeleroCharlotte HuetJorge P. López-AlonsoSandra DelgadoAlexandra DoduEduardo M. BruchLuciano A. AbriataPedro M. AlzariMikel ValleMaría-Natalia LisaNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-8 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Melisa Lázaro Roberto Melero Charlotte Huet Jorge P. López-Alonso Sandra Delgado Alexandra Dodu Eduardo M. Bruch Luciano A. Abriata Pedro M. Alzari Mikel Valle María-Natalia Lisa 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme
description	Lázaro et. al. report the first 3D structure of a large glutamate dehydrogenase (L-GDH), the one corresponding to the Mycobacterium smegmatis enzyme composed of 180 kDa subunits (mL-GDH180), obtained by X-ray crystallography and cryo-electron microscopy. This structure reveals that mL-GDH180 assembles as tetramers with the N- and C-terminal domains being involved in inter-subunit contacts and unveils unique features of the subfamily of L-GDHs.
format	article
author	Melisa Lázaro Roberto Melero Charlotte Huet Jorge P. López-Alonso Sandra Delgado Alexandra Dodu Eduardo M. Bruch Luciano A. Abriata Pedro M. Alzari Mikel Valle María-Natalia Lisa
author_facet	Melisa Lázaro Roberto Melero Charlotte Huet Jorge P. López-Alonso Sandra Delgado Alexandra Dodu Eduardo M. Bruch Luciano A. Abriata Pedro M. Alzari Mikel Valle María-Natalia Lisa
author_sort	Melisa Lázaro
title	3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme
title_short	3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme
title_full	3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme
title_fullStr	3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme
title_full_unstemmed	3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme
title_sort	3d architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/ee3d06ba507e400089d1f6209e598b96
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3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme

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