期刊
FEBS OPEN BIO
卷 7, 期 8, 页码 1208-1216出版社
WILEY
DOI: 10.1002/2211-5463.12260
关键词
allostery; conformational transition; dimerization; phosphotransferase system
资金
- Cooperative Research Program for Agriculture Science & Technology Development, Rural Development Administration [PJ011112]
- Korea Institute of Energy Technology Evaluation and Planning from Ministry of Trade, Industry & Energy, Republic of Korea [20143030090940]
- Korea Evaluation Institute of Industrial Technology (KEIT) [20143030090940] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
The bacterial phosphotransferase system is central to sugar uptake and phosphorylation. Enzyme I (EI), the first enzyme of the system, autophosphorylates as a dimer using phosphoenolpyruvate (PEP), but it is not clearly understood how dimerization activates the enzyme activity. Here, we show that EI dimerization is important for proper conformational transitions and the domain association required for the autophosphorylation. EI(G356S) with reduced dimerization affinity and lower autophosphorylation activity revealed that significantly hindered conformational transitions are required for the phosphoryl transfer reaction. The G356S mutation does not change the binding affinity for PEP, but perturbs the domain association accompanying large interdomain motions that bring the active site His189 close to PEP. The interface for the domain association is separate from the dimerization interface, demonstrating that dimerization can prime the conformational change in an allosteric manner.
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