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Structure of the MazF-mt9 toxin, a tRNA-specific endonuclease from Mycobacterium tuberculosis.
- 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.)
- Subjects :
- Amino Acid Sequence
Apoproteins genetics
Apoproteins metabolism
Bacterial Proteins genetics
Bacterial Proteins metabolism
Bacterial Toxins genetics
Bacterial Toxins metabolism
Base Sequence
Binding Sites
Cloning, Molecular
Endoribonucleases genetics
Endoribonucleases metabolism
Escherichia coli genetics
Escherichia coli metabolism
Gene Expression
Models, Molecular
Mycobacterium tuberculosis enzymology
Mycobacterium tuberculosis pathogenicity
Nucleic Acid Conformation
Protein Binding
Protein Domains
Protein Structure, Secondary
RNA, Transfer, Lys genetics
RNA, Transfer, Lys metabolism
Recombinant Proteins
Sequence Alignment
Structural Homology, Protein
Structure-Activity Relationship
Anticodon chemistry
Apoproteins chemistry
Bacterial Proteins chemistry
Bacterial Toxins chemistry
Endoribonucleases chemistry
Mycobacterium tuberculosis chemistry
RNA, Transfer, Lys chemistry
Subjects
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