6S6X
Structure of Azospirillum brasilense Glutamate Synthase in a6b6 oligomeric state.
Summary for 6S6X
| Entry DOI | 10.2210/pdb6s6x/pdb |
| EMDB information | 10108 |
| Descriptor | Glutamate synthase [NADPH] large chain, Glutamate synthase [NADPH] small chain, FLAVIN MONONUCLEOTIDE, ... (6 entities in total) |
| Functional Keywords | glutamate synthesys, complex, oligomeric assemblies, flavoprotein |
| Biological source | Azospirillum brasilense More |
| Total number of polymer chains | 12 |
| Total formula weight | 1325344.87 |
| Authors | Chaves-Sanjuan, A.,Camilloni, C.,Bolognesi, M. (deposition date: 2019-07-03, release date: 2019-09-11, Last modification date: 2024-05-22) |
| Primary citation | Swuec, P.,Chaves-Sanjuan, A.,Camilloni, C.,Vanoni, M.A.,Bolognesi, M. Cryo-EM Structures of Azospirillum brasilense Glutamate Synthase in Its Oligomeric Assemblies. J.Mol.Biol., 431:4523-4526, 2019 Cited by PubMed Abstract: Bacterial NADPH-dependent glutamate synthase (GltS) is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of two L-Glu molecules from L-Gln and 2-oxo-glutarate. GltS functional unit hosts an α-subunit (αGltS) and a β-subunit (βGltS) that assemble in different αβ oligomers in solution. Here, we present the cryo-electron microscopy structures of Azospirillum brasilense GltS in four different oligomeric states (αβ, αβ, αβ and αβ, in the 3.5- to 4.1-Å resolution range). Our study provides a comprehensive GltS model that details the inter-protomeric assemblies and allows unequivocal location of the FAD cofactor and of two electron transfer [4Fe-4S] clusters within βGltS. PubMed: 31473159DOI: 10.1016/j.jmb.2019.08.011 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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