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TitleAlternative dimerization is required for activity and inhibition of the HEPN ribonuclease RnlA.
Journal, issue, pagesNucleic Acids Res., Vol. 49, Page 7164-7178, Year 2021
Publish dateFeb 17, 2020 (structure data deposition date)
AuthorsGarcia-Rodriguez, G. / Charlier, D. / Wilmaerts, D. / Michiels, J. / Loris, R.
External linksNucleic Acids Res. / PubMed:34139012
MethodsX-ray diffraction
Resolution1.95 - 3.89 Å
Structure data

PDB-6y2p:
Escherichia coli RnlA-RnlB Toxin-Antitoxin System.
Method: X-RAY DIFFRACTION / Resolution: 2.64 Å

PDB-6y2q:
Escherichia coli RnlA endoribonuclease
Method: X-RAY DIFFRACTION / Resolution: 2.99 Å

PDB-6y2r:
Escherichia coli R255A RnlA endoribonuclease (single alanine mutant of RnlA)
Method: X-RAY DIFFRACTION / Resolution: 3.89 Å

PDB-7aex:
NRD-HEPN domains (N-terminal truncation) of Escherichia coli RnlA endoribonuclease
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

Source
  • escherichia coli (strain k12) (bacteria)
KeywordsTOXIN / Prokaryotic Toxin-Antitoxin System / Endoribonuclease / HEPN protein / T4 phage denfense / Antitoxin / Toxin-Antitoxin System / Endoribonuclease catalytic mutant

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