1H, 15N, and 13C backbone assignments and secondary structure of the cytoplasmic domainA of mannitol trasporter IIMannitol from Thermoanaerobacter Tencongensis phosphotransferase system
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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 IIAMtl 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. IIAMtl of Thermoanaerobacter Tencongensis is predicted to have six b strands and six a helices, which is analogous to IIAMtl of Escherichia coli.
Abstract
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 IIAMtl 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. IIAMtl of Thermoanaerobacter Tencongensis is predicted to have six b strands and six a helices, which is analogous to IIAMtl of Escherichia coli.
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