细菌tRNA-（NG37）甲基转移酶N端区域的主链共振归属
Backbone resonance assignment for the N-terminal region of bacterial tRNA-(NG37) methyltransferase.
作者信息
Li Yan, Zhong Wenhe, Koay Ann Zhufang, Ng Hui Qi, Koh-Stenta Xiaoying, Nah Qianhui, Lim Siau Hoi, Larsson Andreas, Lescar Julien, Hill Jeffrey, Dedon Peter C, Kang CongBao
机构信息
Experimental Therapeutics Centre, 31 Biopolis Way, #03-01 Nanos, Singapore, 138669, Singapore.
Department of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, 13 Hangkong Road, Wuhan, Hubei, 430030, People's Republic of China.
出版信息
Biomol NMR Assign. 2019 Apr;13(1):49-53. doi: 10.1007/s12104-018-9849-9. Epub 2018 Oct 8.
Bacterial tRNA (guanine-N)-methyltransferase (TrmD) is an important antibacterial target due to its essential role in translation. TrmD has two domains connected with a flexible linker. The N-terminal domain (NTD) of TrmD contains the S-adenosyl-L-methionine (SAM) cofactor binding site and the C-terminal domain is critical for tRNA binding. Here we report the backbone NMR resonance assignments for NTD of Pseudomonas aeruginosa TrmD. Its secondary structure was determined based on the assigned resonances. Relaxation analysis revealed that NTD existed as dimers in solution. NTD also exhibited thermal stability in solution. Its interactions with SAM and other compounds suggest it can be used for evaluating SAM competitive inhibitors by NMR.
细菌（鸟嘌呤 - N）-甲基转移酶（TrmD）因其在翻译过程中的关键作用而成为重要的抗菌靶点。TrmD有两个通过柔性连接子相连的结构域。TrmD的N端结构域（NTD）包含S-腺苷-L-甲硫氨酸（SAM）辅因子结合位点，C端结构域对tRNA结合至关重要。在此，我们报道了铜绿假单胞菌TrmD的NTD的主链核磁共振共振归属。基于已归属的共振确定了其二级结构。弛豫分析表明NTD在溶液中以二聚体形式存在。NTD在溶液中也表现出热稳定性。它与SAM及其他化合物的相互作用表明可通过核磁共振用于评估SAM竞争性抑制剂。
Zotero 插件