B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state complex
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B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state complex Descriptor: ADENOSINE-5'-DIPHOSPHATE, Glutamine synthetase, L-METHIONINE-S-SULFOXIMINE PHOSPHATE, ... Authors: Schumacher, M.A, Chinnam, N, Tonthat, N, Fisher, S, Wray, L. Deposit date: 2013-07-11 Release date: 2013-11-06 Last modified: 2024-02-28 Method: X-RAY DIFFRACTION (2.5793 Å) Cite: 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, 2013
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2013-07-11



