+検索条件
-Structure paper
タイトル | Cryo-electron microscopy structure of human peroxiredoxin-3 filament reveals the assembly of a putative chaperone. |
---|---|
ジャーナル・号・ページ | Structure, Vol. 23, Issue 5, Page 912-920, Year 2015 |
掲載日 | 2015年5月5日 |
![]() | Mazdak Radjainia / Hariprasad Venugopal / Ambroise Desfosses / Amy J Phillips / N Amy Yewdall / Mark B Hampton / Juliet A Gerrard / Alok K Mitra / ![]() |
PubMed 要旨 | 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- ...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. |
![]() | ![]() ![]() |
手法 | EM (単粒子) |
解像度 | 7.4 Å |
構造データ | ![]() EMDB-6309: |
由来 |
|