Bacterial tRNA (guanine37-N¹)-methyltransferase (TrmD) plays important roles in translation, making it an important target for the development of new antibacterial compounds. TrmD comprises two domains with the N-terminal domain binding to the S-adenosyl-l-methionine (SAM) cofactor and the C-terminal domain critical for tRNA binding. Bacterial TrmD is functional as a dimer. Here we report the backbone NMR resonance assignments for the full length TrmD protein of Pseudomonas aeruginosa. Most resonances were assigned and the secondary structure for each amino acid was determined according to the assigned backbone resonances. The availability of the assignment will be valuable for exploring molecular interactions of TrmD with ligands, inhibitors and tRNA.

中文翻译：

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铜绿假单胞菌的全长tRNA-（N1G37）甲基转移酶的骨干共振分配。

细菌tRNA（鸟嘌呤37-N ¹）-甲基转移酶（TrmD）在翻译中起着重要作用，使其成为开发新型抗菌化合物的重要目标。TrmD包含两个结构域，其N端结构域与S-腺苷-1-甲硫氨酸（SAM）辅因子结合，而C端结构域对tRNA结合至关重要。细菌TrmD可充当二聚体。在这里我们报告的铜绿假单胞菌全长TrmD蛋白的骨架核磁共振共振分配。分配了大多数共振，并根据分配的骨架共振确定了每个氨基酸的二级结构。分配的可用性对于探索TrmD与配体，抑制剂和tRNA的分子相互作用将是有价值的。