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Structural Biology

Study reveals structure of protein that transports body odor precursor

Follow-up studies could lead to inhibitors that block uptake, thus stopping body odor production

by Cici Zhang
July 15, 2018 | APPEARED IN VOLUME 96, ISSUE 29

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Credit: eLife
After a bacterial cell takes up the precursor peptide through this transporter protein, the peptide is converted into a body odor molecule (red) and released outside the cell.

Believe it or not, sweat is odorless. It is bacteria on our underarm skin that feed on unsmelly compounds in sweat and release digestion by-products that are responsible for body odor. Previous research has identified a sulfurous thioalcohol as one of the major body odor molecules. But little is known about how its precursor is taken up by the bacterium Staphylococcus hominis. Now, a team led by Gavin H. Thomas of the University of York and Simon Newstead of the University of Oxford has identified the structure of the protein that transports the body odor precursor peptide into the bacterial cell (eLife 2018, DOI: 10.7554/eLife.34995). When analyzing the transporter’s crystal structure in detail, the researchers found that blocking a long pocket (about 10 Å) that binds the thioalcohol group inhibited the uptake of the body odor precursor. Newstead says this pocket might be used to design specific inhibitors to block body odor production—for example, researchers could design a molecule that plugs this gap and stops the transporter from binding the peptide. European consumer products maker Unilever, which partly funded the study, is assessing the results, Newstead adds.

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