| Title | Cryo-electron microscopy structure of human peroxiredoxin-3 filament reveals the assembly of a putative chaperone |
| Publication Type | Journal Article |
| Year of Publication | 2015 |
| Authors | Radjainia, M., Venugopal H., Desfosses A., Phillips A.J., Yewdall N.A., Hampton M.B., Gerrard J.A., and Mitra A.K. |
| Journal | Structure |
| Volume | 23 |
| Issue | 5 |
| Pagination | 912 - 920 |
| Date Published | 2015 |
| ISSN | 09692126 (ISSN) |
| Abstract | Peroxiredoxins (Prxs) are a ubiquitous class of thiol-dependent peroxidases that play an important role in the protection and response of cells to oxidative stress. The catalytic unit of typical 2-Cys Prxs are homodimers, which can self-associate to form complex assemblies that are hypothesized to have signaling and chaperone activity. Mitochondrial Prx3 forms dodecameric toroids, which can further stack to form filaments, the so-called high-molecular-weight (HMW) form that has putative holdase activity. We used single-particle analysis and helical processing of electron cryomicroscopy images of human Prx3 filaments induced by low pH to generate a ∼7-Å resolution 3D structure of the HMW form, the first such structure for a 2-Cys Prx. The pseudo-atomic model reveals interactions that promote the stacking of the toroids and shows that unlike previously reported data, the structure can accommodate a partially folded C terminus. The HMW filament lumen displays hydrophobic patches, which we hypothesize bestow holdase activity. © 2015 Elsevier Ltd. |
| URL | http://www.scopus.com/inward/record.url?eid=2-s2.0-84930189772&partnerID=40&md5=e91d89096be74f353ff8f8f95bc8a8a8 |
| DOI | 10.1016/j.str.2015.03.019 |
