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-Structure paper
Title | Structure and function analyses of a pertussis-like toxin from pathogenic Escherichia coli reveal a distinct mechanism of inhibition of trimeric G proteins. |
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Journal, issue, pages | J. Biol. Chem., Year 2017 |
Publish date | Apr 10, 2015 (structure data deposition date) |
![]() | 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. ...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. |
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Methods | X-ray diffraction |
Resolution | 1.8 - 2.35 Å |
Structure data | ![]() PDB-4z9c: ![]() PDB-4z9d: |
Chemicals | ![]() ChemComp-PO4: ![]() ChemComp-HOH: ![]() ChemComp-NA: ![]() ChemComp-NAD: |
Source |
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![]() | TRANSFERASE / Redox switch / Pertussis toxin / Typhoid toxin / ADP-ribosyltransferase / Escherichia coli / AB5 / UTEC / pertussis like / Membrane glycoproteins / Toxin / Plt / PltAB / PltA / ribosyltransferase |