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

The mannitol transporter Enzyme IIMtl of the bacterial phosphotransferase system has two cytoplasmic phosphoryl transfer domains IIAMtl and IIBMtl. 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 a helices, which is analogous to IIA(Mtl) of Escherichia coli.