Clare College Cambridge

Dr Andrew Carter

 

Director of Studies (Part IA) Biological Sciences

Fellow of Clare College 

 

http://www2.mrc-lmb.cam.ac.uk/groups/cartera/main.html

If you look at any of the cells in your body you would see that its contents is continuously moved around.  This transport is important for the function and survival of the cell and is driven by tiny motor proteins.  One of these motor proteins is called dynein, it transports a vast number of cargos and is medically relevant as it is hijacked by many viruses which use it to get into the center of the cell.  However dynein is also much larger and more complex than the other motor proteins and so until recently it has been difficult to study.  We are interested in determining the structure, how the atoms that make up the protein are arranged, of different parts of dynein.  To do this we purify the dynein protein from bakers yeast (Saccharomyce cerevisiae), persuade it to form tiny crystals and then analyse them with a very intense beam of X-rays: a process called X-ray crystallography.  

Knowing the structure of dynein will tell us how it uses the energy from breaking down ATP molecules to drive movement and how it manages to carry so many different cargos at different times to different places.   It will also help us understand how viruses are able to manipulate dynein into transporting them.

 

"Dynein walking out of the darkness: an artistic rendering of dynein motor proteins walking along microtubules, based upon our X-ray crystal structure.  This work reveals the architecture of this molecular machine that powers ciliary beating and intracellular transport and provides insight into how ATP hydrolysis energy is converted into motion (Carter AP et al, 2011, Science 331, 1159). Image created by Graham Johnson of TSRI and grahamj.com."