7mft | pdb_00007mft

Glutamate synthase, glutamate dehydrogenase counter-enzyme complex (GudB6-GltA6-GltB6)

spinqualitylabelsall models 7mft, resolution 3.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7mft is a 3 chain structure with sequence from Bacillus subtilis subsp. subtilis NCIB 3610 = ATCC 6051 = DSM 10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.9Å Ligands: F3S, FAD, FMN, SF4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GUDB_BACSU GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon source in the absence of arginine. It is unable to synthesize glutamate. Publication Abstract from PubMed Multi-enzyme assemblies composed of metabolic enzymes catalyzing sequential reactions are being increasingly studied. Here, we report the discovery of a 1.6 megadalton multi-enzyme complex from Bacillus subtilis composed of two enzymes catalyzing opposite ('counter-enzymes') rather than sequential reactions: glutamate synthase (GltAB) and glutamate dehydrogenase (GudB), which make and break glutamate, respectively. In vivo and in vitro studies show that the primary role of complex formation is to inhibit the activity of GudB. Using cryo-electron microscopy, we elucidated the structure of the complex and the molecular basis of inhibition of GudB by GltAB. The complex exhibits unusual oscillatory progress curves and is necessary for both planktonic growth, in glutamate-limiting conditions, and for biofilm growth, in glutamate-rich media. The regulation of a key metabolic enzyme by complexing with its counter enzyme may thus enable cell growth under fluctuating glutamate concentrations. A counter-enzyme complex regulates glutamate metabolism in Bacillus subtilis.,Jayaraman V, Lee DJ, Elad N, Vimer S, Sharon M, Fraser JS, Tawfik DS Nat Chem Biol. 2022 Feb;18(2):161-170. doi: 10.1038/s41589-021-00919-y. Epub 2021 , Dec 20. PMID:34931064 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutamate dehydrogenase 3D structures Glutamate synthase

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