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

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

doi:10.1038/s42003-021-02222-x

Communications Biology (Jun 2021)

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

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

Affiliations

Melisa Lázaro: Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A
Roberto Melero: Centro Nacional de Biotecnología, CNB-CSIC, Darwin 3
Charlotte Huet: Unité de Microbiologie Structurale, Institut Pasteur, CNRS UMR 3528, Université de Paris, 25 rue du Docteur Roux
Jorge P. López-Alonso: Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A
Sandra Delgado: Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A
Alexandra Dodu: Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A
Eduardo M. Bruch: Integrated Structural Biology Department, IGBMC, 1 Rue Laurent Fries
Luciano A. Abriata: Laboratory for Biomolecular Modeling, School of Life Sciences, École Polytechnique Fédérale de Lausanne and Swiss Institute of Bioinformatics
Pedro M. Alzari: Unité de Microbiologie Structurale, Institut Pasteur, CNRS UMR 3528, Université de Paris, 25 rue du Docteur Roux
Mikel Valle: Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A
María-Natalia Lisa: Unité de Microbiologie Structurale, Institut Pasteur, CNRS UMR 3528, Université de Paris, 25 rue du Docteur Roux

DOI: https://doi.org/10.1038/s42003-021-02222-x
Journal volume & issue: Vol. 4, no. 1
pp. 1 – 8

Abstract

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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.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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