4LNN

B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of apo form of GS

Summary for 4LNN

Entry DOI	10.2210/pdb4lnn/pdb
Related	4LNF 4LNI 4LNK 4LNO
Descriptor	Glutamine synthetase, MAGNESIUM ION, SULFATE ION, ... (4 entities in total)
Functional Keywords	glutamine synthetase, enzyme, dodecamer, alpha/beta, ligase
Biological source	Bacillus subtilis
Cellular location	Cytoplasm: P12425
Total number of polymer chains	12
Total formula weight	603570.81
Authors	Schumacher, M.A.,Chinnam, N.,Tonthat, N.,Fisher, S.,Wray, L. (deposition date: 2013-07-11, release date: 2013-11-13, Last modification date: 2023-09-20)
Primary citation	Murray, D.S.,Chinnam, N.,Tonthat, N.K.,Whitfill, T.,Wray, L.V.,Fisher, S.H.,Schumacher, M.A. Structures of the Bacillus subtilis Glutamine Synthetase Dodecamer Reveal Large Intersubunit Catalytic Conformational Changes Linked to a Unique Feedback Inhibition Mechanism. J.Biol.Chem., 288:35801-35811, 2013 Cited by PubMed: 24158439 DOI: 10.1074/jbc.M113.519496 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.1 Å)

Structure validation