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The antibacterial toxin colicin N binds to the inner core of lipopolysaccharide and close to its translocator protein.

Johnson CL, Ridley H, Marchetti R, Silipo A, Griffin DC, Crawford L, Bonev B, Molinaro A, Lakey JH - Mol. Microbiol. (2014)

Bottom Line: Delipidated LPS (LPS(Δ) (LIPID) ) shows weaker binding; and thus full affinity requires the lipid component.The site of LPS binding means that ColN will preferably bind at the interface and thus position itself close to the surface of its translocon component, OmpF.ColN is, currently, unique among colicins in requiring LPS and, combined with previous data, this implies that the ColN translocon is distinct from those of other known colicins.

View Article: PubMed Central - PubMed

Affiliation: Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University, Framlington Place, Newcastle-upon-Tyne, NE2 4HH, UK.

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STD NMR data for ColN‐R binding to Rc LPSΔLIPID and Rd LPSΔLIPID.A. Reference 1H‐NMR spectrum (a) and 1D STD NMR spectrum (b) of mixed colicin: Rc LPSΔLIPID 1:100.B. Reference 1H NMR spectrum (a) and 1D STD NMR spectrum (b) of mixed colicin: Rd LPSΔLIPID 1:100.C. STD‐derived epitope mapping of the ColN‐R:RcLPSΔLIPID interaction with colour coding from the highest (red) to lowest (yellow) observed STD effect.
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mmi12568-fig-0004: STD NMR data for ColN‐R binding to Rc LPSΔLIPID and Rd LPSΔLIPID.A. Reference 1H‐NMR spectrum (a) and 1D STD NMR spectrum (b) of mixed colicin: Rc LPSΔLIPID 1:100.B. Reference 1H NMR spectrum (a) and 1D STD NMR spectrum (b) of mixed colicin: Rd LPSΔLIPID 1:100.C. STD‐derived epitope mapping of the ColN‐R:RcLPSΔLIPID interaction with colour coding from the highest (red) to lowest (yellow) observed STD effect.

Mentions: C. PDB structures of (a) ColN (1A87) colouring as above and missing the disordered 90 residues of the T‐domain. Showing the residues mutated to cysteines to form the disulphide bridge (V94 and Q179) as space filling. Also at the same scale a representative LPS structure equivalent to Rd plus Hep(III) (see Fig. 4) from the structure of the TLR4‐MD‐2‐E. coli LPS complex 3FXI (Park et al., 2009).


The antibacterial toxin colicin N binds to the inner core of lipopolysaccharide and close to its translocator protein.

Johnson CL, Ridley H, Marchetti R, Silipo A, Griffin DC, Crawford L, Bonev B, Molinaro A, Lakey JH - Mol. Microbiol. (2014)

STD NMR data for ColN‐R binding to Rc LPSΔLIPID and Rd LPSΔLIPID.A. Reference 1H‐NMR spectrum (a) and 1D STD NMR spectrum (b) of mixed colicin: Rc LPSΔLIPID 1:100.B. Reference 1H NMR spectrum (a) and 1D STD NMR spectrum (b) of mixed colicin: Rd LPSΔLIPID 1:100.C. STD‐derived epitope mapping of the ColN‐R:RcLPSΔLIPID interaction with colour coding from the highest (red) to lowest (yellow) observed STD effect.
© Copyright Policy - creativeCommonsBy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4114557&req=5

mmi12568-fig-0004: STD NMR data for ColN‐R binding to Rc LPSΔLIPID and Rd LPSΔLIPID.A. Reference 1H‐NMR spectrum (a) and 1D STD NMR spectrum (b) of mixed colicin: Rc LPSΔLIPID 1:100.B. Reference 1H NMR spectrum (a) and 1D STD NMR spectrum (b) of mixed colicin: Rd LPSΔLIPID 1:100.C. STD‐derived epitope mapping of the ColN‐R:RcLPSΔLIPID interaction with colour coding from the highest (red) to lowest (yellow) observed STD effect.
Mentions: C. PDB structures of (a) ColN (1A87) colouring as above and missing the disordered 90 residues of the T‐domain. Showing the residues mutated to cysteines to form the disulphide bridge (V94 and Q179) as space filling. Also at the same scale a representative LPS structure equivalent to Rd plus Hep(III) (see Fig. 4) from the structure of the TLR4‐MD‐2‐E. coli LPS complex 3FXI (Park et al., 2009).

Bottom Line: Delipidated LPS (LPS(Δ) (LIPID) ) shows weaker binding; and thus full affinity requires the lipid component.The site of LPS binding means that ColN will preferably bind at the interface and thus position itself close to the surface of its translocon component, OmpF.ColN is, currently, unique among colicins in requiring LPS and, combined with previous data, this implies that the ColN translocon is distinct from those of other known colicins.

View Article: PubMed Central - PubMed

Affiliation: Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University, Framlington Place, Newcastle-upon-Tyne, NE2 4HH, UK.

Show MeSH
Related in: MedlinePlus