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Yorodumi- PDB-7mfm: Glutamate synthase, glutamate dehydrogenase counter-enzyme complex -
+Open data
-Basic information
Entry | Database: PDB / ID: 7mfm | |||||||||
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Title | Glutamate synthase, glutamate dehydrogenase counter-enzyme complex | |||||||||
Components |
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Keywords | CYTOSOLIC PROTEIN / Counter-enzyme complex / glutamate synthase / glutamate dehydrogenae | |||||||||
Function / homology | Function and homology information glutamate synthase activity / oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor / glutamate biosynthetic process / glutamate dehydrogenase (NAD+) activity / glutamate catabolic process / 3 iron, 4 sulfur cluster binding / glutamine metabolic process / iron-sulfur cluster binding / nucleotide binding / metal ion binding Similarity search - Function | |||||||||
Biological species | Bacillus subtilis (bacteria) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.42 Å | |||||||||
Authors | Jayaraman, V. / Lee, D.J. / Elad, N. / Fraser, J.S. / Tawfik, D.S. | |||||||||
Funding support | Israel, United States, 2items
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Citation | Journal: Nat Chem Biol / Year: 2022 Title: A counter-enzyme complex regulates glutamate metabolism in Bacillus subtilis. Authors: Vijay Jayaraman / D John Lee / Nadav Elad / Shay Vimer / Michal Sharon / James S Fraser / Dan S Tawfik / Abstract: 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 ...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. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 7mfm.cif.gz | 2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb7mfm.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 7mfm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7mfm_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 7mfm_full_validation.pdf.gz | 1.3 MB | Display | |
Data in XML | 7mfm_validation.xml.gz | 149.9 KB | Display | |
Data in CIF | 7mfm_validation.cif.gz | 234.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mf/7mfm ftp://data.pdbj.org/pub/pdb/validation_reports/mf/7mfm | HTTPS FTP |
-Related structure data
Related structure data | 23817MC 7mftC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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