7A1D
Cryo-EM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis (open conformation)
Summary for 7A1D
| Entry DOI | 10.2210/pdb7a1d/pdb |
| EMDB information | 11606 |
| Descriptor | NAD-specific glutamate dehydrogenase (1 entity in total) |
| Functional Keywords | large glutamate dehydrogenase mycobacterium metabolism, oxidoreductase |
| Biological source | Mycolicibacterium smegmatis MC2 155 |
| Total number of polymer chains | 4 |
| Total formula weight | 705367.44 |
| 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: 2020-08-12, 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 Cited by 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: 34083757DOI: 10.1038/s42003-021-02222-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.19 Å) |
Structure validation
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