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Structure paper

TitleStructural and kinetic insights into stimulation of RppH-dependent RNA degradation by the metabolic enzyme DapF.
Journal, issue, pagesNucleic Acids Res., Vol. 46, Page 6841-6856, Year 2018
Publish dateApr 11, 2018 (structure data deposition date)
AuthorsGao, A. / Vasilyev, N. / Luciano, D.J. / Levenson-Palmer, R. / Richards, J. / Marsiglia, W.M. / Traaseth, N.J. / Belasco, J.G. / Serganov, A.
External linksNucleic Acids Res. / PubMed:29733359
MethodsX-ray diffraction
Resolution1.81 - 3.06 Å
Structure data

PDB-6d13:
Crystal structure of E.coli RppH-DapF complex
Method: X-RAY DIFFRACTION / Resolution: 3.06 Å

PDB-6d1q:
Crystal structure of E. coli RppH-DapF complex, monomer
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-6d1v:
Crystal structure of E. coli RppH-DapF complex, monomer bound to RNA
Method: X-RAY DIFFRACTION / Resolution: 1.81 Å

Chemicals

ChemComp-IOD:
IODIDE ION

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-MG:
Unknown entry

Source
  • escherichia coli o45:k1 (strain s88 / expec) (bacteria)
  • escherichia coli (strain k12) (bacteria)
  • escherichia coli (E. coli)
Keywordsisomerase/hydrolase / RNA decay / DapF / RppH / isomerase-hydrolase complex / isomerase/hydrolase/rna / isomerase-hydrolase-rna complex

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