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1H, 13C and 15N resonance assignments of RNA pyrophosphohydrolase RppH from Escherichia coli
- Source :
- Biomolecular NMR assignments. 3(1)
- Publication Year :
- 2009
-
Abstract
- The mRNA degradation is an important regulatory mechanism which controls gene expression by limiting the number of translation times. Previous studies demonstrated that this process is essential for organisms. Escherichia coli RNA pyrophosphohydrolase (RppH) is an enzyme that triggers mRNA degradation by removing the 5' pyrophosphate, which is a rate-determining step. In order to understand the molecular mechanism of the biological function, the structural information of RppH is required. Herein, we report the resonance assignments of (1)H, (15)N, (13)C atoms of the E. coli RppH.
- Subjects :
- Magnetic Resonance Spectroscopy
Molecular Sequence Data
Biology
medicine.disease_cause
Biochemistry
Pyrophosphate
chemistry.chemical_compound
Structural Biology
MRNA degradation
Gene expression
medicine
Amino Acid Sequence
Escherichia coli
chemistry.chemical_classification
Carbon Isotopes
Nitrogen Isotopes
Escherichia coli Proteins
RNA
Translation (biology)
Acid Anhydride Hydrolases
Protein Structure, Tertiary
Protein Subunits
Enzyme
chemistry
Molecular mechanism
Protons
Subjects
Details
- ISSN :
- 1874270X
- Volume :
- 3
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Biomolecular NMR assignments
- Accession number :
- edsair.doi.dedup.....903da229b2a20c896aba7ccc649bc28b