Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.
Journal, issue, pages	Nat Commun, Vol. 13, Issue 1, Page 3793, Year 2022
Publish date	Jul 1, 2022
Authors	Brady A Travis / Jared V Peck / Raul Salinas / Brandon Dopkins / Nicholas Lent / Viet D Nguyen / Mario J Borgnia / Richard G Brennan / Maria A Schumacher /
PubMed Abstract	How bacteria sense and respond to nitrogen levels are central questions in microbial physiology. In Gram-positive bacteria, nitrogen homeostasis is controlled by an operon encoding glutamine ...How bacteria sense and respond to nitrogen levels are central questions in microbial physiology. In Gram-positive bacteria, nitrogen homeostasis is controlled by an operon encoding glutamine synthetase (GS), a dodecameric machine that assimilates ammonium into glutamine, and the GlnR repressor. GlnR detects nitrogen excess indirectly by binding glutamine-feedback-inhibited-GS (FBI-GS), which activates its transcription-repression function. The molecular mechanisms behind this regulatory circuitry, however, are unknown. Here we describe biochemical and structural analyses of GS and FBI-GS-GlnR complexes from pathogenic and non-pathogenic Gram-positive bacteria. The structures show FBI-GS binds the GlnR C-terminal domain within its active-site cavity, juxtaposing two GlnR monomers to form a DNA-binding-competent GlnR dimer. The FBI-GS-GlnR interaction stabilizes the inactive GS conformation. Strikingly, this interaction also favors a remarkable dodecamer to tetradecamer transition in some GS, breaking the paradigm that all bacterial GS are dodecamers. These data thus unveil unique structural mechanisms of transcription and enzymatic regulation.
External links	Nat Commun / PubMed:35778410 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.96 - 3.5 Å
Structure data	25863 7tf6 EMDB-25863, PDB-7tf6: S. aureus GS(12)-Q-GlnR peptide Method: EM (single particle) / Resolution: 2.15 Å 25864 7tf7 EMDB-25864, PDB-7tf7: S. aureus GS(12) - apo Method: EM (single particle) / Resolution: 2.13 Å 25866 7tf9 EMDB-25866, PDB-7tf9: L. monocytogenes GS(14)-Q-GlnR peptide Method: EM (single particle) / Resolution: 2.61 Å 25867 7tfa EMDB-25867, PDB-7tfa: P. polymyxa GS(12)-Q-GlnR peptide Method: EM (single particle) / Resolution: 2.07 Å 25868 7tfb EMDB-25868, PDB-7tfb: P. polymyxa GS(14)-Q-GlnR peptide Method: EM (single particle) / Resolution: 2.28 Å 25869 7tfc EMDB-25869, PDB-7tfc: B. subtilis GS(14)-Q-GlnR peptide Method: EM (single particle) / Resolution: 1.96 Å 25870 7tfd EMDB-25870, PDB-7tfd: P. polymyxa GS(12) - apo Method: EM (single particle) / Resolution: 3.16 Å 25871 7tfe EMDB-25871, PDB-7tfe: L. monocytogenes GS(12) - apo Method: EM (single particle) / Resolution: 2.85 Å PDB-7tdp: Structure of Paenibacillus polymyxa GS bound to Met-Sox-P-ADP (Transition state complex) to 1.98 Angstom Method: X-RAY DIFFRACTION / Resolution: 1.98 Å PDB-7tdv: Crystal structure of S. aureus glutamine synthetase in Met-Sox-P/ADP transition state complex Method: X-RAY DIFFRACTION / Resolution: 2.92 Å PDB-7tea: Crystal structure of S. aureus GlnR-DNA complex Method: X-RAY DIFFRACTION / Resolution: 2.35 Å PDB-7tec: Structure of the Listeria monocytogenes GlnR-DNA complex to 3.45 Angstrom Method: X-RAY DIFFRACTION / Resolution: 3.45 Å PDB-7ten: Crystal structure of the Listeria monocytogenes GS-Met-Sox-P- ADP complex to 3.5 Angstrom Method: X-RAY DIFFRACTION / Resolution: 3.5 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-P3S: L-METHIONINE-S-SULFOXIMINE PHOSPHATE ChemComp-MG: Unknown entry ChemComp-HOH: WATER / Water ChemComp-SO4: SULFATE ION / Sulfate ChemComp-CA: Unknown entry ChemComp-GLN*: GLUTAMINE / Glutamine
Source	staphylococcus aureus (bacteria) listeria monocytogenes (bacteria) paenibacillus polymyxa (bacteria) bacillus subtilis (bacteria) synthetic construct (others)
Keywords	LIGASE / glutamate-ammonium ligase / GlnR / GS / feedback inhibition / transcription coregulator / glnRA / Glutamine synthetase / S. aureus / femC / DNA BINDING PROTEIN/DNA / winged-HTH / transcription repressor / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex / listeria / repressor / transcription / LIGASE/INHIBITOR / glutamate ammonium ligase / Met-Sox / transition state / LIGASE-INHIBITOR complex / BIOSYNTHETIC PROTEIN / glutamine synthetase repressor dodecamer / glutamine synthetase dodecamer / glutamine synthetase repressor tetradecamer