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Backbone Assignment of Phosphorylated Cytoplasmic Domain B of Mannitol Transporter IIMtl in Thermoanaerobacter Tengcongensis  

Lee, Ko On (Department of Agricultural Biotechnology, Seoul National University)
Suh, Jeong-Yong (Department of Agricultural Biotechnology, Seoul National University)
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Journal of the Korean Magnetic Resonance Society / v.21, no.1, 2017 , pp. 20-25 More about this Journal
The cytoplasmic domains A and B of the mannitol transporter enzyme $II^{Mtl}$ are covalently linked in Escherichia coli, but separately expressed in Thermoanaerobacter Tengcongensis. The phosphorylation of domain B ($TtIIB^{Mtl}$) substantially increases the binding affinity to the domain A ($TtIIA^{Mtl}$) in T. Tengcongensis. To understand the structural basis of the enhanced domain-domain interaction by protein phosphorylation, we obtained NMR backbone assignments of the phospho-$TtIIB^{Mtl}$ using a standard suite of triple resonance experiments. Our results will be useful to monitor chemical shift changes at the active site of phosphorylation and the binding interfaces.
backbone assignment; mannitol transporter Enzyme II; phosphorylated protein Thermoanaerobacter Tengcongensis;
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