7P4Y
GlnK2 from Methanothermococcus thermolithotrophicus in the apo state at a resolution of 2.3 A
This is a non-PDB format compatible entry.
Summary for 7P4Y
| Entry DOI | 10.2210/pdb7p4y/pdb |
| Descriptor | GlnK2 from Methanothermococcus thermolithotrophicus, CHLORIDE ION (3 entities in total) |
| Functional Keywords | pii-family protein, protein inhibitor, regulation, methanococcales, methanogenic archaea, thermophile, atp binding, 2-oxoglutarate, conformational changes, t-loop, nitrogen-metabolism, signaling protein |
| Biological source | Methanothermococcus thermolithotrophicus DSM 2095 |
| Total number of polymer chains | 12 |
| Total formula weight | 177209.07 |
| Authors | Mueller, M.-C.,Wagner, T. (deposition date: 2021-07-13, release date: 2021-10-06, Last modification date: 2024-01-31) |
| Primary citation | Muller, M.C.,Wagner, T. The Oxoglutarate Binding Site and Regulatory Mechanism Are Conserved in Ammonium Transporter Inhibitors GlnKs from Methanococcales . Int J Mol Sci, 22:-, 2021 Cited by PubMed Abstract: Protein inhibition is a natural regulatory process to control cellular metabolic fluxes. P-family signal-transducing effectors are in this matter key regulators of the nitrogen metabolism. Their interaction with their various targets is governed by the cellular nitrogen level and the energy charge. Structural studies on GlnK, a P-family inhibitor of the ammonium transporters (Amt), showed that the T-loops responsible for channel obstruction are displaced upon the binding of 2-oxoglutarate, magnesium and ATP in a conserved cleft. However, GlnK from was shown to bind 2-oxoglutarate on the tip of its T-loop, causing a moderate disruption to GlnK-Amt interaction, raising the question if methanogenic archaea use a singular adaptive strategy. Here we show that membrane fractions of released GlnKs only in the presence of Mg-ATP and 2-oxoglutarate. This observation led us to structurally characterize the two GlnK isoforms apo or in complex with ligands. Together, our results show that the 2-oxoglutarate binding interface is conserved in GlnKs from , including , emphasizing the importance of a free carboxy-terminal group to facilitate ligand binding and to provoke the shift of the T-loop positions. PubMed: 34445335DOI: 10.3390/ijms22168631 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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