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Structure paper

TitleDapF stabilizes the substrate-favoring conformation of RppH to stimulate its RNA-pyrophosphohydrolase activity in Escherichia coli.
Journal, issue, pagesNucleic Acids Res., Vol. 46, Page 6880-6892, Year 2018
Publish dateSep 27, 2017 (structure data deposition date)
AuthorsWang, Q. / Zhang, D. / Guan, Z. / Li, D. / Pei, K. / Liu, J. / Zou, T. / Yin, P.
External linksNucleic Acids Res. / PubMed:29931175
MethodsX-ray diffraction
Resolution2.298 Å
Structure data

PDB-5ygu:
Crystal structure of Escherichia coli (strain K12) mRNA Decapping Complex RppH-DapF
Method: X-RAY DIFFRACTION / Resolution: 2.298 Å

Chemicals

ChemComp-TLA:
L(+)-TARTARIC ACID

ChemComp-IOD:
IODIDE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (strain k12) (bacteria)
  • escherichia coli (E. coli)
KeywordsISOMERASE/HYDROLASE / RppH-DapF / Decapping / Hydrolase / ISOMERASE-HYDROLASE complex

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