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

Authors :
Chen R
Tu J
Liu Z
Meng F
Ma P
Ding Z
Yang C
Chen L
Deng X
Xie W
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2017 May 06; Vol. 486 (3), pp. 804-810. Date of Electronic Publication: 2017 Mar 25.
Publication Year :
2017

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 tRNA <superscript>Lys</superscript> 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.<br /> (Copyright © 2017 Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1090-2104
Volume :
486
Issue :
3
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
28351618
Full Text :
https://doi.org/10.1016/j.bbrc.2017.03.132