How to keep proteins protected from holes

See allHide authors and affiliations

Science  14 Aug 2015:
Vol. 349, Issue 6249, pp. 702-703
DOI: 10.1126/science.349.6249.702-g

Many enzymes are a little like circus performers juggling torches: They make highly reactive fragments that they then steer toward the intended targets, without getting burned themselves along the way. Gray and Winkler now present a hypothesis to account for some measure of enzymes' capacity for self-preservation from oxidative damage. They systematically surveyed structures in the Protein Data Bank to search for chains of three or more tyrosine and tryptophan residues in contexts where oxidation chemistry might be at play. The prevalence of these motifs suggests that the aromatic amino acids might shuttle positive holes (ensuing from oxidative electron transfer) from a fragile region of the protein to a safer site.

Proc. Natl. Acad. Sci. U.S.A. 10.1073/pnas.1512704112 (2015).

Navigate This Article