5GUD
Glutamate dehydrogenase from Corynebacterium glutamicum (alpha-iminoglutarate/NADP+ complex)
Summary for 5GUD
| Entry DOI | 10.2210/pdb5gud/pdb |
| Descriptor | Glutamate dehydrogenase, (2Z)-2-iminopentanedioic acid, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total) |
| Functional Keywords | rossmann fold, glutamate dehydrogenase, oxidoreductase |
| Biological source | Corynebacterium glutamicum |
| Total number of polymer chains | 6 |
| Total formula weight | 316389.15 |
| Authors | Tomita, T.,Nishiyama, M. (deposition date: 2016-08-28, release date: 2017-06-07, Last modification date: 2023-11-08) |
| Primary citation | Tomita, T.,Yin, L.,Nakamura, S.,Kosono, S.,Kuzuyama, T.,Nishiyama, M. Crystal structure of the 2-iminoglutarate-bound complex of glutamate dehydrogenase from Corynebacterium glutamicum FEBS Lett., 591:1611-1622, 2017 Cited by PubMed Abstract: The NADP -dependent glutamate dehydrogenase from Corynebacterium glutamicum (CgGDH) is considered to be one of the key enzymes in the industrial fermentation of glutamate due to its high glutamate-producing activity. We determined the crystal structure of CgGDH complexed with NADP and 2-iminoglutarate. Among six subunits of hexameric CgGDH-binding NADP , only four subunits bind 2-iminoglutarate in a closed form, while the other two are in an open form. In the closed form, 2-iminoglutarate is bound to the substrate-binding site with the 2-imino group stacked by the nicotinamide ring of the coenzyme, suggesting a prehydride transfer state in a hypothesized reaction scheme with the imino intermediate. We also conducted MD simulations and provide insights into the extreme preference for the glutamate-producing reaction of CgGDH. PubMed: 28486765DOI: 10.1002/1873-3468.12667 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.68 Å) |
Structure validation
Download full validation report
