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Structure paper

TitleStructure of a novel antibacterial toxin that exploits elongation factor Tu to cleave specific transfer RNAs.
Journal, issue, pagesNucleic Acids Res., Vol. 45, Page 10306-10320, Year 2017
Publish dateFeb 12, 2016 (structure data deposition date)
AuthorsMichalska, K. / Gucinski, G.C. / Garza-Sanchez, F. / Johnson, P.M. / Stols, L.M. / Eschenfeldt, W.H. / Babnigg, G. / Low, D.A. / Goulding, C.W. / Joachimiak, A. / Hayes, C.S.
External linksNucleic Acids Res. / PubMed:28973472
MethodsX-ray diffraction
Resolution2.35 - 3.3 Å
Structure data

PDB-5i4q:
Contact-dependent inhibition system from Escherichia coli NC101 - ternary CdiA/CdiI/EF-Tu complex (domains 2 and 3)
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

PDB-5i4r:
Contact-dependent inhibition system from Escherichia coli NC101 - ternary CdiA/CdiI/EF-Tu complex (trypsin-modified)
Method: X-RAY DIFFRACTION / Resolution: 3.3 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

Source
  • escherichia coli nc101 (bacteria)
  • escherichia coli (E. coli)
KeywordsTOXIN/ANTITOXIN / toxin / antitoxin / elongation factor / Structural Genomics / PSI-Biology / Midwest Center for Structural Genomics / MCSG / Structure-Function Analysis of Polymorphic CDI Toxin-Immunity Protein Complexes / UC4CDI / TOXIN-ANTITOXIN complex

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