7JSR

Crystal structure of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis

Summary for 7JSR

• Entry DOI: 10.2210/pdb7jsr/pdb
• Related: 7A1D
• Descriptor: NAD-specific glutamate dehydrogenase (1 entity in total)
• Functional Keywords: large glutamate dehydrogenase, mycobacterium, metabolism, oxidoreductase
• Biological source: Mycolicibacterium smegmatis
• Total number of polymer chains: 2
• Total formula weight: 355309.78

Authors

Lazaro, M.,Melero, R.,Huet, C.,Lopez-Alonso, J.P.,Delgado, S.,Dodu, A.,Bruch, E.M.,Abriata, L.A.,Alzari, P.M.,Valle, M.,Lisa, M.N. (deposition date: 2020-08-15, release date: 2021-06-09, Last modification date: 2025-05-14)

Primary citation

Lazaro, M.,Melero, R.,Huet, C.,Lopez-Alonso, J.P.,Delgado, S.,Dodu, A.,Bruch, E.M.,Abriata, L.A.,Alzari, P.M.,Valle, M.,Lisa, M.N.
3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme.
Commun Biol, 4:684-684, 2021

PubMed 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) contain long N- and C-terminal segments flanking the catalytic core. Despite the relevance of L-GDHs 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 (mL-GDH) adopts a quaternary structure that is radically different from that of related low molecular weight enzymes. Intersubunit contacts in mL-GDH 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.

PubMed: 34083757
DOI: 10.1038/s42003-021-02222-x

Experimental method

X-RAY DIFFRACTION (6.27 Å)