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4LNF

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

Summary for 4LNF
Entry DOI10.2210/pdb4lnf/pdb
Related4LNI 4LNK 4LNN 4LNO
DescriptorGlutamine synthetase, MAGNESIUM ION, GLUTAMINE, ... (5 entities in total)
Functional Keywordsglutamine synthetase, gs, enzyme, alpha-beta, tnra, glnr-dna, ligase
Biological sourceBacillus subtilis
Cellular locationCytoplasm: P12425
Total number of polymer chains12
Total formula weight605491.46
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 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 (2.949 Å)
Structure validation

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