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Resonance assignment of the 128 kDa enzyme I dimer from Thermoanaerobacter tengcongensis

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Abstract

Enzyme I (EI) of the bacterial phosphotransferase system (PTS) utilizes phosphoenolpyruvate (PEP) as a source of energy in order to transport sugars across the cellular membrane. PEP binding to EI initiates a phosphorylation cascade that regulates a variety of essential pathways in the metabolism of bacterial cells. Given its central role in controlling bacterial metabolism, EI has been often suggested as a good target for antimicrobial research. Here, we report the 1HN, 15N, 13C′, 1Hmethyl, and 13Cmethyl chemical shifts of the 128 kDa homodimer EI from the thermophile Thermoanaerobacter tengcongensis. In total 79% of the expected backbone amide correlations and 80% of the expected methyl TROSY peaks from U-[2H, 13C, 15N], Ileδ1-[13CH3], Val-Leu-[13CH3/12CD3] labeled EI were assigned. The reported assignments will enable future structural studies aimed at illuminating the fundamental mechanisms governing long-range interdomain communication in EI and at indicating new therapeutic strategies to combat bacterial infections.

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Acknowledgements

This work was supported by funds from the Roy J. Carver Charitable Trust and Iowa State University (to V.V.).

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Authors and Affiliations

  1. Department of Chemistry, Iowa State University, Hach Hall, 2438 Pammel Drive, Ames, IA, 50011, USA

    Rochelle Rea Dotas & Vincenzo Venditti

  2. Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, 50011, USA

    Vincenzo Venditti

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  1. Rochelle Rea Dotas
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  2. Vincenzo Venditti
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Correspondence to Vincenzo Venditti.

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Dotas, R.R., Venditti, V. Resonance assignment of the 128 kDa enzyme I dimer from Thermoanaerobacter tengcongensis. Biomol NMR Assign 13, 287–293 (2019). https://doi.org/10.1007/s12104-019-09893-y

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