1H, 15N, and 13C backbone assignments and secondary structure of the cytoplasmic domain A of mannitol trasporter IIMannitol from Thermoanaerobacter Tencongensis phosphotransferase system

  • Lee, Ko-On (Department of Agricultural Biotechnology, College of Agriculture and Life Sciences, Seoul National University) ;
  • Suh, Jeong-Yong (Department of Agricultural Biotechnology, College of Agriculture and Life Sciences, Seoul National University)
  • Received : 2015.05.04
  • Accepted : 2015.06.03
  • Published : 2015.06.30


The mannitol transporter Enzyme $II^{Mtl}$ of the bacterial phosphotransferase system has two cytoplasmic phosphoryl transfer domains $IIA^{Mtl}$ and $IIB^{Mtl}$. The two domains are linked by a flexible peptide linker in mesophilic bacterial strains, whereas they are expressed as separated domains in thermophilic strains. Here, we carried out backbone assignment of $IIA^{Mtl}$ from thermophilic Thermoanaerobacter Tencongensis using a suite of heteronuclear triple resonance NMR spectroscopy. We have completed 94% of the backbone assignment, and obtained secondary structural information based on torsion angles derived from the chemical shifts. $IIA^{Mtl}$ of Thermoanaerobacter Tencongensis is predicted to have six ${\beta}$ strands and six ${\alpha}$ helices, which is analogous to $IIA^{Mtl}$ of Escherichia coli.



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