9DA9
Crystal structure of GluN1/GluN2A agonist-binding domains in complex with 7CKA and glutamate
Summary for 9DA9
| Entry DOI | 10.2210/pdb9da9/pdb |
| Descriptor | Glutamate receptor ionotropic, NMDA 1, Glutamate receptor ionotropic, NMDA 2A, 7-Chlorokynurenic acid, ... (5 entities in total) |
| Functional Keywords | glutamate receptor ligand-gated ion channel neurotransmitter receptor synaptic transmission neuropharmacology, signaling protein |
| Biological source | Rattus norvegicus (Norway rat) More |
| Total number of polymer chains | 2 |
| Total formula weight | 65496.07 |
| Authors | Bosco, J.,Yates-Hansen, C.K.,McClelland, L.J.,Voronina, E.,Hansen, K.B. (deposition date: 2024-08-22, release date: 2025-03-12, Last modification date: 2025-04-16) |
| Primary citation | Bosco, J.,Gagliano, E.,Boshae, K.L.,Statz, J.P.,Wheeler, T.B.,Cuello, D.,Sliter, A.,Newby, C.,Lin, B.,Demeler, A.,Pierpont, C.L.,Yates-Hansen, C.,Sydor, M.J.,Ferrini, M.E.,Kuch, K.C.,Cooper, B.S.,Piggott, B.J.,Certel, S.J.,Hansen, K.B.,Sprang, S.R.,Bowler, B.,McClelland, L.,Berkmen, M.,Voronina, E. A galactose-based auto-expression system improves T7-inducible protein production in Escherichia coli. Sci Rep, 15:8936-8936, 2025 Cited by PubMed Abstract: Protein production using Escherichia coli is a cornerstone of modern biotechnology. In this study, we developed a novel auto-expression medium to maximize protein production. Each E. coli strain tested was capable of auto-expression in response to galactose, including strains in which the endogenous lacZ had been disrupted. This provides key evidence that galactose can regulate the lac operon independent of known lac operon-regulated metabolism. The enhanced capabilities of the novel auto-expression medium were documented across protein production systems including (1) increased yields for routinely expressed proteins (e.g. eGFP), (2) improved expression of human cytochrome c within a dual expression system, (3) robust auto-expression in lacZ-deficient strains producing proteins with challenging disulfide bonds, and (4) reproducible 8-fold increase in SpCas9 yields, at ≥ 95% purity. This novel medium can streamline production and improve yields for routine as well as challenging proteins, accelerating recombinant protein production and creating new opportunities in biotechnology and structural biology. PubMed: 40089537DOI: 10.1038/s41598-025-91954-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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