3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme - Archive ouverte HAL Access content directly
Journal Articles Communications Biology Year : 2021

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

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Abstract

Glutamate dehydrogenases (GDHs) are widespread metabolic enzymes that play key roles in nitrogen homeostasis. Large glutamate dehydrogenases composed of 180 kDa subunits (L-GDHs 180) contain long N-and C-terminal segments flanking the catalytic core. Despite the relevance of L-GDHs 180 in bacterial physiology, the lack of structural data for these enzymes has limited the progress of functional studies. Here we show that the mycobacterial L-GDH 180 (mL-GDH 180) adopts a quaternary structure that is radically different from that of related low molecular weight enzymes. Intersubunit contacts in mL-GDH 180 involve a C-terminal domain that we propose as a new fold and a flexible N-terminal segment comprising ACT-like and PAS-type domains that could act as metabolic sensors for allosteric regulation. These findings uncover unique aspects of the structure-function relationship in the subfamily of L-GDHs.
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Dates and versions

hal-03878750 , version 1 (30-11-2022)

Licence

Attribution - CC BY 4.0

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Cite

Melisa Lázaro, Roberto Melero, Charlotte Huet, Jorge P López-Alonso, Sandra Delgado, et al.. 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. Communications Biology, 2021, 4 (1), pp.684. ⟨10.1038/s42003-021-02222-x⟩. ⟨hal-03878750⟩
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