7MFM
Glutamate synthase, glutamate dehydrogenase counter-enzyme complex
This is a non-PDB format compatible entry.
Summary for 7MFM
| Entry DOI | 10.2210/pdb7mfm/pdb |
| EMDB information | 23817 |
| Descriptor | Glutamate dehydrogenase, Glutamate synthase (NADPH) large chain, Glutamate synthase (NADPH) small chain, ... (7 entities in total) |
| Functional Keywords | counter-enzyme complex, glutamate synthase, glutamate dehydrogenae, cytosolic protein |
| Biological source | Bacillus subtilis More |
| Total number of polymer chains | 10 |
| Total formula weight | 741120.17 |
| Authors | Jayaraman, V.,Lee, D.J.,Elad, N.,Fraser, J.S.,Tawfik, D.S. (deposition date: 2021-04-10, release date: 2022-01-05, Last modification date: 2024-12-25) |
| Primary citation | Jayaraman, V.,Lee, D.J.,Elad, N.,Vimer, S.,Sharon, M.,Fraser, J.S.,Tawfik, D.S. A counter-enzyme complex regulates glutamate metabolism in Bacillus subtilis. Nat.Chem.Biol., 18:161-170, 2022 Cited by PubMed Abstract: Multi-enzyme assemblies composed of metabolic enzymes catalyzing sequential reactions are being increasingly studied. Here, we report the discovery of a 1.6 megadalton multi-enzyme complex from Bacillus subtilis composed of two enzymes catalyzing opposite ('counter-enzymes') rather than sequential reactions: glutamate synthase (GltAB) and glutamate dehydrogenase (GudB), which make and break glutamate, respectively. In vivo and in vitro studies show that the primary role of complex formation is to inhibit the activity of GudB. Using cryo-electron microscopy, we elucidated the structure of the complex and the molecular basis of inhibition of GudB by GltAB. The complex exhibits unusual oscillatory progress curves and is necessary for both planktonic growth, in glutamate-limiting conditions, and for biofilm growth, in glutamate-rich media. The regulation of a key metabolic enzyme by complexing with its counter enzyme may thus enable cell growth under fluctuating glutamate concentrations. PubMed: 34931064DOI: 10.1038/s41589-021-00919-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.42 Å) |
Structure validation
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