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 ¹H_N, ¹⁵N, ¹³C′, ¹H_methyl, and ¹³C_methyl 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], Ile^δ1-[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.

中文翻译：

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腾康热厌氧杆菌128 kDa酶I二聚体的共振分配。

细菌磷酸转移酶系统（PTS）的酶I（EI）利用磷酸烯醇丙酮酸（PEP）作为能量来源，以使糖跨细胞膜转运。PEP与EI结合会启动磷酸化级联反应，从而调节细菌细胞代谢中的多种基本途径。鉴于其在控制细菌代谢中的核心作用，EI通常被认为是抗微生物研究的良好靶标。在这里，我们报道了嗜热嗜热厌氧细菌腾康的128 kDa同型二聚体EI的¹ H _N，¹⁵ N，¹³ C'，¹ H_甲基和¹³ C_甲基化学位移。总计来自U- [ ² H，¹³ C，¹⁵ N]，^Ileδ1- [ ¹³ CH ₃ ]，Val-Leu- [ ¹³ CH _3的79％预期主链酰胺相关性和80％预期甲基TROSY峰/ ¹² CD ₃ ]标记为EI。所报告的任务将使未来的结构研究能够阐明在EI中控制远程域间通信的基本机制，并指出对抗细菌感染的新治疗策略。