4JML
Crystal structure of the TolB(P201C)-ColicinE9 TBE peptide(A33C) complex.
Summary for 4JML
| Entry DOI | 10.2210/pdb4jml/pdb |
| Related | 2ivz |
| Descriptor | Protein TolB, Colicin-E9, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | protein-protein interaction, engineered disulfide, bacteriocin transport, protein transport, protein transport-toxin complex, protein transport/toxin |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 2 |
| Total formula weight | 46396.33 |
| Authors | Wojdyla, J.A.,Klein, A.,Kleanthous, C. (deposition date: 2013-03-14, release date: 2013-07-17, Last modification date: 2024-11-20) |
| Primary citation | Housden, N.G.,Hopper, J.T.,Lukoyanova, N.,Rodriguez-Larrea, D.,Wojdyla, J.A.,Klein, A.,Kaminska, R.,Bayley, H.,Saibil, H.R.,Robinson, C.V.,Kleanthous, C. Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF. Science, 340:1570-1574, 2013 Cited by PubMed Abstract: Porins are β-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. Formation of the translocon involved ColE9's unstructured N-terminal domain threading in opposite directions through two OmpF subunits, capturing its target TolB on the other side of the membrane in a fixed orientation that triggers colicin import. Thus, an intrinsically disordered protein can tunnel through the narrow pores of an oligomeric porin to deliver an epitope signal to the cell to initiate cell death. PubMed: 23812713DOI: 10.1126/science.1237864 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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