4LNO

B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: form two of GS-1

Summary for 4LNO

• Entry DOI: 10.2210/pdb4lno/pdb
• Related: 4LNF 4LNI 4LNK 4LNN
• Descriptor: Glutamine synthetase, MAGNESIUM ION, GLUTAMINE, ... (4 entities in total)
• Functional Keywords: alpha/beta, tnra, glnr, ligase
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm: P12425
• Total number of polymer chains: 6
• Total formula weight: 302409.96

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; PubMed: 24158439; DOI: 10.1074/jbc.M113.519496

Experimental method

X-RAY DIFFRACTION (2.9 Å)