7W85
Structural of the filamentous Escherichia coli glutamine synthetase
This is a non-PDB format compatible entry.
Summary for 7W85
| Entry DOI | 10.2210/pdb7w85/pdb |
| EMDB information | 32352 |
| Descriptor | Glutamine synthetase, NICKEL (II) ION (2 entities in total) |
| Functional Keywords | glutamine synthetase, filament, biosynthetic protein |
| Biological source | Escherichia coli BL21(DE3) |
| Total number of polymer chains | 24 |
| Total formula weight | 1249663.72 |
| Authors | Huang, P.-C.,Chen, S.-K.,Wu, K.-P. (deposition date: 2021-12-07, release date: 2022-04-06, Last modification date: 2024-06-26) |
| Primary citation | Huang, P.C.,Chen, S.K.,Chiang, W.H.,Ho, M.R.,Wu, K.P. Structural basis for the helical filament formation of Escherichia coli glutamine synthetase. Protein Sci., 31:e4304-e4304, 2022 Cited by PubMed Abstract: Escherichia coli glutamine synthetase (EcGS) spontaneously forms a dodecamer that catalytically converts glutamate to glutamine. EcGS stacks with other dodecamers to create a filament-like polymer visible under transmission electron microscopy. Filamentous EcGS is induced by environmental metal ions. We used cryo-electron microscopy (cryo-EM) to decipher the structure of metal ion (nickel)-induced EcGS helical filament at a sub-3Å resolution. EcGS filament formation involves stacking of native dodecamers by chelating nickel ions to residues His5 and His13 in the first N-terminal helix (H1). His5 and His13 from paired parallel H1 helices provide salt bridges and hydrogen bonds to tightly stack two dodecamers. One subunit of the EcGS filament hosts two nickel ions, whereas the dodecameric interface and the ATP/Mg-binding site both host a nickel ion each. We reveal that upon adding glutamate or ATP for catalytic reactions, nickel-induced EcGS filament reverts to individual dodecamers. Such tunable filament formation is often associated with stress responses. Our results provide detailed structural information on the mechanism underlying reversible and tunable EcGS filament formation. PubMed: 35481643DOI: 10.1002/pro.4304 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.94 Å) |
Structure validation
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