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Title | Cryo-EM Structures of Azospirillum brasilense Glutamate Synthase in Its Oligomeric Assemblies. |
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Journal, issue, pages | J Mol Biol, Vol. 431, Issue 22, Page 4523-4526, Year 2019 |
Publish date | Nov 8, 2019 |
Authors | Paolo Swuec / Antonio Chaves-Sanjuan / Carlo Camilloni / Maria Antonietta Vanoni / Martino Bolognesi / |
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 ...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. |
External links | J Mol Biol / PubMed:31473159 |
Methods | EM (single particle) |
Resolution | 3.5 - 4.1 Å |
Structure data | EMDB-10104, PDB-6s6s: EMDB-10105, PDB-6s6t: EMDB-10106, PDB-6s6u: EMDB-10108, PDB-6s6x: |
Chemicals | ChemComp-FMN: ChemComp-F3S: ChemComp-SF4: ChemComp-FAD: |
Source |
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Keywords | FLAVOPROTEIN / glutamate synthesys / complex / oligomeric assemblies |