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4LNI

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

Summary for 4LNI
Entry DOI10.2210/pdb4lni/pdb
Related4LNF 4LNK 4LNN 4LNO
DescriptorGlutamine synthetase, L-METHIONINE-S-SULFOXIMINE PHOSPHATE, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
Functional Keywordsalpha-beta, tnra, glnra, ligase
Biological sourceBacillus subtilis
Total number of polymer chains12
Total formula weight611606.72
Authors
Schumacher, M.A.,Chinnam, N.,Tonthat, N.,Fisher, S.,Wray, L. (deposition date: 2013-07-11, release date: 2013-11-06, Last modification date: 2024-02-28)
Primary citationMurray, 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 (2.5793 Å)
Structure validation

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