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Structure of the MazF-mt9 toxin, a tRNA-specific endonuclease from Mycobacterium tuberculosis

Author:
Chen, Ran, Tu, Jie, Liu, Zhihui, Meng, Fanrong, Ma, Pinyun, Ding, Zhishan, Yang, Chengwen, Chen, Lei, Deng, Xiangyu, Xie, Wei
Source:
Biochemical and biophysical research communications 2017
ISSN:
0006-291X
Subject:
Mycobacterium tuberculosis, catalytic activity, crystal structure, proteins, transfer RNA, tuberculosis
Abstract:
Tuberculosis (TB) is a severe disease caused by Mycobacterium tuberculosis (M. tb) and the well-characterized M. tb MazE/F proteins play important roles in stress adaptation. Recently, the MazF-mt9 toxin has been found to display endonuclease activities towards tRNAs but the mechanism is unknown. We hereby present the crystal structure of apo-MazF-mt9. The enzyme recognizes tRNALys with a central UUU motif within the anticodon loop, but is insensitive to the sequence context outside of the loop. Based on our crystallographic and biochemical studies, we identified key residues for catalysis and proposed the potential tRNA-binding site.
Agid:
5657032