1H, 13C and 15N resonance assignments of RNA pyrophosphohydrolase RppH from Escherichia coli.
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.
Bi
Yunchen
Y
Beijing Nuclear Magnetic Resonance Center, Peking University, 100871, Beijing, China.
Li
Hongwei
H
Fan
Shoujin
S
Xia
Bin
B
Jin
Changwen
C
D017766:Acid Anhydride Hydrolases / Q000737:chemistry*; D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D029968:Escherichia coli Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011522:Protons
D002247:Carbon Isotopes; D029968:Escherichia coli Proteins; D009587:Nitrogen Isotopes; D021122:Protein Subunits; D011522:Protons; D017766:Acid Anhydride Hydrolases; C526730:RppH protein, E coli