4lni

B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state complex

spinqualitylabelsall models 4lni, resolution 2.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4lni is a 12 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5793Å Ligands: ADP, MG, P3S Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLN1A_BACSU Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism (PubMed:25691471). It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia (PubMed:24158439). Feedback-inhibited GlnA interacts with and regulates the activity of the transcriptional regulator TnrA (PubMed:11719184, PubMed:12139611). During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation (PubMed:11719184, PubMed:12139611, PubMed:25691471). Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity (PubMed:11719184, PubMed:12139611, PubMed:25691471). In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes (PubMed:25691471). See Also Glutamine synthetase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA