8TFB
Cryo-EM structure of the Methanosarcina mazei apo glutamin synthetase structure: dodecameric form
This is a non-PDB format compatible entry.
Summary for 8TFB
| Entry DOI | 10.2210/pdb8tfb/pdb |
| EMDB information | 41228 |
| Descriptor | Glutamine synthetase, MAGNESIUM ION (2 entities in total) |
| Functional Keywords | glutamine sythetase, gs, methanosarcina mazei, apo, dodecamer, ligase |
| Biological source | Methanosarcina mazei |
| Total number of polymer chains | 12 |
| Total formula weight | 634226.77 |
| Authors | Schumacher, M.A. (deposition date: 2023-07-09, release date: 2023-11-15, Last modification date: 2023-11-29) |
| Primary citation | Schumacher, M.A.,Salinas, R.,Travis, B.A.,Singh, R.R.,Lent, N. M. mazei glutamine synthetase and glutamine synthetase-GlnK1 structures reveal enzyme regulation by oligomer modulation. Nat Commun, 14:7375-7375, 2023 Cited by PubMed Abstract: Glutamine synthetases (GS) play central roles in cellular nitrogen assimilation. Although GS active-site formation requires the oligomerization of just two GS subunits, all GS form large, multi-oligomeric machines. Here we describe a structural dissection of the archaeal Methanosarcina mazei (Mm) GS and its regulation. We show that Mm GS forms unstable dodecamers. Strikingly, we show this Mm GS oligomerization property is leveraged for a unique mode of regulation whereby labile Mm GS hexamers are stabilized by binding the nitrogen regulatory protein, GlnK1. Our GS-GlnK1 structure shows that GlnK1 functions as molecular glue to affix GS hexamers together, stabilizing formation of GS active-sites. These data, therefore, reveal the structural basis for a unique form of enzyme regulation by oligomer modulation. PubMed: 37968329DOI: 10.1038/s41467-023-43243-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.99 Å) |
Structure validation
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