Cryo-EM Structures of Azospirillum brasilense Glutamate Synthase in Its Oligomeric Assemblies. 2019

Paolo Swuec, and Antonio Chaves-Sanjuan, and Carlo Camilloni, and Maria Antonietta Vanoni, and Martino Bolognesi
Dipartimento di Bioscienze, Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy; Centro di Ricerca Pediatrica Romeo ed Enrica Invernizzi, Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy.

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 (α4β3, α4β4, α6β4 and α6β6, 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]+1,+2 clusters within βGltS.

UI MeSH Term Description Entries
D007506 Iron-Sulfur Proteins A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation. Iron-Sulfur Protein,Iron Sulfur Proteins,Iron Sulfur Protein,Protein, Iron-Sulfur,Proteins, Iron Sulfur,Proteins, Iron-Sulfur,Sulfur Proteins, Iron
D002384 Catalysis The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction. Catalyses
D004579 Electron Transport The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270) Respiratory Chain,Chain, Respiratory,Chains, Respiratory,Respiratory Chains,Transport, Electron
D005182 Flavin-Adenine Dinucleotide A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972) FAD,Flavitan,Dinucleotide, Flavin-Adenine,Flavin Adenine Dinucleotide
D005486 Flavin Mononucleotide A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues. FMN,Flavin Mononucleotide Disodium Salt,Flavin Mononucleotide Monosodium Salt,Flavin Mononucleotide Monosodium Salt, Dihydrate,Flavin Mononucleotide Sodium Salt,Riboflavin 5'-Monophosphate,Riboflavin 5'-Phosphate,Riboflavin Mononucleotide,Sodium Riboflavin Phosphate,5'-Monophosphate, Riboflavin,5'-Phosphate, Riboflavin,Mononucleotide, Flavin,Mononucleotide, Riboflavin,Phosphate, Sodium Riboflavin,Riboflavin 5' Monophosphate,Riboflavin 5' Phosphate,Riboflavin Phosphate, Sodium
D005970 Glutamate Synthase An enzyme that catalyzes the formation of 2 molecules of glutamate from glutamine plus alpha-ketoglutarate in the presence of NADPH. EC 1.4.1.13. Glutamine Ketoglutarate Amidotransferase,Ketoglutarate Glutamine Amidotransferase,Amidotransferase, Glutamine Ketoglutarate,Amidotransferase, Ketoglutarate Glutamine,Glutamine Amidotransferase, Ketoglutarate,Ketoglutarate Amidotransferase, Glutamine,Synthase, Glutamate
D015806 Azospirillum brasilense A species of motile, free-living, gram-negative bacteria that occur in the soil. They are aerobic or microaerophilic and are sometimes capable of nitrogen fixation. Azospirillum brasiliense,Roseomonas fauriae,Spirillum lipoferum
D020285 Cryoelectron Microscopy Electron microscopy involving rapid freezing of the samples. The imaging of frozen-hydrated molecules and organelles permits the best possible resolution closest to the living state, free of chemical fixatives or stains. Electron Cryomicroscopy,Cryo-electron Microscopy,Cryo electron Microscopy,Cryo-electron Microscopies,Cryoelectron Microscopies,Cryomicroscopies, Electron,Cryomicroscopy, Electron,Electron Cryomicroscopies,Microscopies, Cryo-electron,Microscopies, Cryoelectron,Microscopy, Cryo-electron,Microscopy, Cryoelectron

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