Friday, 6 March 2015

Bacterial crystal structure

Two crystal structures for translocator protein (TSPO)—from the bacteria Bacillus cereus and Rhodobacter sphaeroides—are the latest pieces in the puzzle that is determining the functions of this integral mitochondrial membrane protein. The structures, published in the journal Science, are a match, but they differ from a published murine TSPO.

“Membrane proteins are very difficult to work on . . . so when you have two independent groups actually coming up with seemingly identical or very similar structures, it’s very gratifying,” said structural biologist Chris Tate of the Medical Research Council’s Laboratory of Molecular Biology in Cambridge, UK, who was not involved in the studies.

“This protein is 5 billion years old, so it has been evolving over all that time and has adapted to the various needs of the tissues, cells, and species. . . . It’s not surprising that it may really have diverse roles,” Vasillios Papadopoulos, a professor of medicine at McGill University in Montreal stated.

For more on this interesting research, see The Scientist.

Posted by Tim Sandle