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1H, 13C, and 15N backbone and side-chain chemical shift assignment of the staphylococcal MazF mRNA interferase
- Source :
- Vrije Universiteit Brussel
- Publication Year :
- 2011
- Publisher :
- Springer Science and Business Media LLC, 2011.
-
Abstract
- MazF proteins are ribonucleases that cleave mRNA with high sequence-specificity as part of bacterial stress response and that are neutralized by the action of the corresponding antitoxin MazE. Prolonged activation of the toxin MazF leads to cell death. Several mazEF modules from gram-negative bacteria have been characterized in terms of catalytic activity, auto-regulation mechanism and structure, but less is known about their distant relatives found in gram-positive organisms. Currently, no solution NMR structure is available for any wild-type MazF toxin. Here we report the (1)H, (15)N and (13)C backbone and side-chain chemical shift assignments of this toxin from the pathogen bacterium Staphylococcus aureus. The BMRB accession number is 17288.
- Subjects :
- Staphylococcus aureus
Bacterial Toxins
Molecular Sequence Data
medicine.disease_cause
Biochemistry
Microbiology
Ribonucleases
Bacterial Proteins
Structural Biology
Side chain
medicine
Amino Acid Sequence
Nuclear Magnetic Resonance, Biomolecular
Pathogen
Carbon Isotopes
Messenger RNA
Nitrogen Isotopes
biology
Toxin
Accession number (library science)
biology.organism_classification
Recombinant Proteins
NMR
macromolecular complex
Antitoxin
Toxin-Antitoxin module
Sequence Alignment
Bacteria
MazF
Subjects
Details
- ISSN :
- 1874270X and 18742718
- Volume :
- 5
- Database :
- OpenAIRE
- Journal :
- Biomolecular NMR Assignments
- Accession number :
- edsair.doi.dedup.....2fce53ad7c30dd1c61c1e12aa943c960
- Full Text :
- https://doi.org/10.1007/s12104-010-9290-1