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TitleStructure and function analyses of a pertussis-like toxin from pathogenic Escherichia coli reveal a distinct mechanism of inhibition of trimeric G proteins.
Journal, issue, pagesJ. Biol. Chem., Year 2017
Publish dateApr 10, 2015 (structure data deposition date)
AuthorsLittler, D.R. / Ang, S.Y. / Moriel, D.G. / Kocan, M. / Kleifeld, O. / Johnson, M.D. / Tran, M.T. / Paton, A.W. / Paton, J.C. / Summers, R. ...Littler, D.R. / Ang, S.Y. / Moriel, D.G. / Kocan, M. / Kleifeld, O. / Johnson, M.D. / Tran, M.T. / Paton, A.W. / Paton, J.C. / Summers, R. / Schrembri, M. / Rossjohn, J. / Beddoe, T.T.
External linksJ. Biol. Chem. / PubMed:28663369
MethodsX-ray diffraction
Resolution1.8 - 2.35 Å
Structure data

PDB-4z9c:
EcPltAB Oxidized
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

PDB-4z9d:
EcPltA
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / Redox switch / Pertussis toxin / Typhoid toxin / ADP-ribosyltransferase / Escherichia coli / AB5 / UTEC / pertussis like / Membrane glycoproteins / Toxin / Plt / PltAB / PltA / ribosyltransferase

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