4LNK
B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-glutamate-AMPPCP complex
Summary for 4LNK
Entry DOI | 10.2210/pdb4lnk/pdb |
Related | 4LNF 4LNI 4LNN 4LNO |
Descriptor | Glutamine synthetase, GLUTAMIC ACID, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total) |
Functional Keywords | alpha-beta, ligase |
Biological source | Bacillus subtilis |
Total number of polymer chains | 6 |
Total formula weight | 305267.26 |
Authors | Schumacher, M.A.,Chinnam, N.,Tonthat, N.,Fisher, S.,Wray, L. (deposition date: 2013-07-11, release date: 2013-10-30, 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: 24158439DOI: 10.1074/jbc.M113.519496 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.87 Å) |
Structure validation
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