Cute molecules and the scientists who adore them: Sarah Gharbi
Sarah Gharbi, technician at EMBL Grenoble, talks about her favourite protein complex, which looks like a poodle
Sarah Gharbi from EMBL Grenoble says that the Bhogaraju group describes this protein complex (PDB 8QFS) as a poodle, with a very unusual shape for a protein complex: it has a head (the E.coli elongation factor protein), a muzzle (the tRNA), a body (SidH), and even a flexible tail, like a dog! Credit: Isabel Romero Calvo (illustration), Mylène André (photography)/EMBL
The cute side of science
Behind every discovery lies a story. Often this story is of a scientist and their passion and awe for nature’s design.
We’ve asked some of our scientists, from across EMBL sites, to talk about the molecules that capture their imaginations and make them smile. These stories reveal the surprising beauty, humour, and charm in the molecular structures that power life itself. We invite you to explore them and fall in love with the molecules, like these scientists have.
“Looking at proteins is like looking at clouds, the shape we see can be quite subjective. But I think we can all agree that this protein looks like a poodle!
“It’s our group’s ‘pet molecule’: this poodle is a molecular complex, which comprises SidH, a toxin from Legionella pneumophila (the body), bound to the E. coli elongation factor protein (the head), and tRNA (the muzzle). Most other such complexes are globular, but this one has ‘legs’ and a flexible ‘tail’ like a dog, which makes it very unusual.
“The structure of this complex was solved by Rahul Sharma, a former postdoctoral researcher in our group, with the help of, among others, our former PhD student Simonne Griffith-Jones. I supported the study by creating cellular tools so that the researchers could study the functionality of SidH – quite a challenging task because of the toxicity of the protein. The initial idea was that SidH inhibits protein translation, but the study found no evidence of that. However, mutations in the region of SidH responsible for binding to tRNA/elongation factor reduce the toxicity of SidH in human cells, suggesting that this region is important for the toxicity of the protein.”
Sarah Gharbi (France), Research Technician, Bhogaraju Group, EMBL Grenoble
