1LLZ
Structural studies on the synchronization of catalytic centers in glutamate synthase: reduced enzyme
Summary for 1LLZ
| Entry DOI | 10.2210/pdb1llz/pdb |
| Related | 1LLW 1LM1 |
| Descriptor | Ferredoxin-dependent glutamate synthase, FLAVIN MONONUCLEOTIDE, FE3-S4 CLUSTER (3 entities in total) |
| Functional Keywords | glutamate synthase, channeling, amidotransferase, oxidoreductase |
| Biological source | Synechocystis sp. PCC 6803 |
| Total number of polymer chains | 1 |
| Total formula weight | 166463.83 |
| Authors | van den Heuvel, R.H.,Ferrari, D.,Bossi, R.T.,Ravasio, S.,Curti, B.,Vanoni, M.A.,Florencio, F.J.,Mattevi, A. (deposition date: 2002-04-30, release date: 2002-07-31, Last modification date: 2023-10-25) |
| Primary citation | van den Heuvel, R.H.,Ferrari, D.,Bossi, R.T.,Ravasio, S.,Curti, B.,Vanoni, M.A.,Florencio, F.J.,Mattevi, A. Structural studies on the synchronization of catalytic centers in glutamate synthase J.BIOL.CHEM., 277:24579-24583, 2002 Cited by PubMed Abstract: The complex iron-sulfur flavoprotein glutamate synthase (GltS) plays a prominent role in ammonia assimilation in bacteria, yeasts, and plants. GltS catalyzes the formation of two molecules of l-glutamate from 2-oxoglutarate and l-glutamine via intramolecular channeling of ammonia. GltS has the impressive ability of synchronizing its distinct catalytic centers to avoid wasteful consumption of l-glutamine. We have determined the crystal structure of the ferredoxin-dependent GltS in several ligation and redox states. The structures reveal the crucial elements in the synchronization between the glutaminase site and the 2-iminoglutarate reduction site. The structural data combined with the catalytic properties of GltS indicate that binding of ferredoxin and 2-oxoglutarate to the FMN-binding domain of GltS induce a conformational change in the loop connecting the two catalytic centers. The rearrangement induces a shift in the catalytic elements of the amidotransferase domain, such that it becomes activated. This machinery, over a distance of more than 30 A, controls the ability of the enzyme to bind and hydrolyze the ammonia-donating substrate l-glutamine. PubMed: 11967268DOI: 10.1074/jbc.M202541200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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