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TitleCryo-electron microscopy structure of human peroxiredoxin-3 filament reveals the assembly of a putative chaperone.
Journal, issue, pagesStructure, Vol. 23, Issue 5, Page 912-920, Year 2015
Publish dateMay 5, 2015
AuthorsMazdak Radjainia / Hariprasad Venugopal / Ambroise Desfosses / Amy J Phillips / N Amy Yewdall / Mark B Hampton / Juliet A Gerrard / Alok K Mitra /
PubMed AbstractPeroxiredoxins (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- ...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.
External linksStructure / PubMed:25914057
MethodsEM (single particle)
Resolution7.4 Å
Structure data

EMDB-6309:
Cryo-EM structure of human peroxiredoxin-3 filament reveals the assembly of a putative chaperone
Method: EM (single particle) / Resolution: 7.4 Å

Source
  • Homo sapiens (human)

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