Structural survey of the peroxiredoxins

Abstract

Peroxiredoxins (Prxs) are ubiquitous proteins that use an active site Cys residue to reduce hydroperoxides. Structural studies since the first Prx structure was determined in 1998 have produced 35 crystal structures of wild type and mutant Prxs with at least one representative structure from each of the five major evolutionary subfamilies of Prxs. These structures have yielded a great deal of knowledge about Prx structure and structure-function relations, revealing fascinating variations in quaternary structure and details of the fully-folded and locally-unfolded conformations that are involved in the catalytic cycle of all Prxs.