Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 486, Issue 3, Pages 804-810Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2017.03.132
Keywords
Crystal structure; Toxin-antitoxin; tRNA endonuclease; Structure-function; Substrate specificity
Categories
Funding
- Fundamental Research Funds for the Central Universities [161gjc76]
- Science and Technology Program of Guangzhou [201504010025, 155700012, 2014Y2-00117, 201605030012]
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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. (C) 2017 Elsevier Inc. All rights reserved.
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