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-Structure paper
Title | Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF. |
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Journal, issue, pages | Science, Vol. 340, Issue 6140, Page 1570-1574, Year 2013 |
Publish date | Jun 28, 2013 |
Authors | Nicholas G Housden / Jonathan T S Hopper / Natalya Lukoyanova / David Rodriguez-Larrea / Justyna A Wojdyla / Alexander Klein / Renata Kaminska / Hagan Bayley / Helen R Saibil / Carol V Robinson / Colin Kleanthous / |
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) ...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. |
External links | Science / PubMed:23812713 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 2 - 20.0 Å |
Structure data | EMDB-2372: PDB-4jml: |
Chemicals | ChemComp-CA: ChemComp-HOH: |
Source |
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Keywords | PROTEIN TRANSPORT/TOXIN / protein-protein interaction / engineered disulfide / bacteriocin transport / protein transport / PROTEIN TRANSPORT-TOXIN complex |