Department of Biochemistry University of Oxford Department of Biochemistry
University of Oxford
South Parks Road
Oxford OX1 3QU

Tel: +44 (0)1865 613200
Fax: +44 (0)1865 613201
Anaphase bridges in fission yeast cells
Whitby lab
Lactose permease represented using bending cylinders in Bendix software
Caroline Dahl, Sansom lab
Epithelial cells in C. elegans showing a seam cell that failed to undergo cytokinesis
Serena Ding, Woollard lab
Collage of Drosophila third instar larva optic lobe
Lu Yang, Davis lab
First year Biochemistry students at a practical class
Image showing the global movement of lipids in a model planar membrane
Matthieu Chavent, Sansom lab
Bootstrap Slider

Simulations contribute to study on critical bacterial outer membrane protein

Molecular dynamics simulations by Dr Phillip Stansfeld in the lab of Professor Mark Sansom have helped to reveal how bacteria construct a barrier against antibiotics and the body's immune system.

This player requires Flash or an HTML 5 capable browser

Movie illustrating the simulated opening of the side-gate of the LptDE structure through which lipopolysaccharide is inserted into the membrane. Copyright Phillip Stansfeld

These fortifications are found in Gram-negative bacteria which cause many different infections including salmonella, pseudomonas and meningitis. By impeding the construction of this barrier, it might be possible to tackle antibiotic-resistant bacteria.

Dr Stansfeld provided molecular dynamics simulations for a structural study carried out by groups from the University of East Anglia and Diamond Light Source. The researchers have published their work in Nature (1).

They describe the first crystal structure of the unique membrane lipopolysaccharide translocon in these bacteria. The LptD-LptE complex builds up the outer membrane, acting as a biological ‘bricklayer’ that pulls up the lipopolysaccharide 'bricks' from inside the bacterium to insert them in the outer membrane. 

Simulations of the LptD-LptE complex helped the researchers understand the lipopolysaccharide translocation mechanism by indicating how the barrel within the translocon opens to allow membrane insertion.

You can find more information about the work on the Diamond and BBC websites.

  1. Structural basis for outer membrane lipopolysaccharide insertion. Dong, H. et. al. Nature (2014) June 18 doi:10.1038/nature13464

 

 

 

Search

 

Share This