Structural highlights
Publication Abstract from PubMed
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 alpha-subunit (alphaGltS) and a beta-subunit (betaGltS) that assemble in different alphabeta oligomers in solution. Here, we present the cryo-electron microscopy structures of Azospirillum brasilense GltS in four different oligomeric states (alpha4beta3, alpha4beta4, alpha6beta4 and alpha6beta6, in the 3.5- to 4.1-A 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 betaGltS.
Cryo-EM Structures of Azospirillum brasilense Glutamate Synthase in Its Oligomeric Assemblies.,Swuec P, Chaves-Sanjuan A, Camilloni C, Vanoni MA, Bolognesi M J Mol Biol. 2019 Aug 29. pii: S0022-2836(19)30520-0. doi:, 10.1016/j.jmb.2019.08.011. PMID:31473159[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Swuec P, Chaves-Sanjuan A, Camilloni C, Vanoni MA, Bolognesi M. Cryo-EM Structures of Azospirillum brasilense Glutamate Synthase in Its Oligomeric Assemblies. J Mol Biol. 2019 Aug 29. pii: S0022-2836(19)30520-0. doi:, 10.1016/j.jmb.2019.08.011. PMID:31473159 doi:http://dx.doi.org/10.1016/j.jmb.2019.08.011
