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Krios II-Titan Krios II at Diamond	3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme Melisa Lazaro , Roberto Melero , Charlotte Huet , Jorge Lopez-Alonso , Sandra Delgado , Alexandra Dodu , Eduardo M. Bruch , Luciano A. Abriata , Pedro M. Alzari , Mikel Valle , María-Natalia Lisa Communications Biology 4 DOI: 10.1038/s42003-021-02222-x Diamond Proposal Number(s): [14743] Open Access Show Abstract ▼ Abstract: Glutamate dehydrogenases (GDHs) are widespread metabolic enzymes that play key roles in nitrogen homeostasis. Large glutamate dehydrogenases composed of 180 kDa subunits (L-GDHs180) contain long N- and C-terminal segments flanking the catalytic core. Despite the relevance of L-GDHs180 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-GDH180 (mL-GDH180) adopts a quaternary structure that is radically different from that of related low molecular weight enzymes. Intersubunit contacts in mL-GDH180 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.	Jun 2021

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