Prx3 Oligomeric Structure Click the buttons to change the display
Dimer --> As typical 2-Cys Prxs, individual protomers of Prx3 form dimers via the B-interface.  The CP is red and the CR is grey.

Ring --> Dimers bind to each other via the A-interface to form dodecamer rings.  Other Prxs form different size rings. 

Asp74, Ser75, and Ser78 are important for the A-interface.  These residues are colored lime green.

Filament --> Rings bind to each other via the R-interface.  This may help the rings stay together during the catalytic cycle when the A-interface is destabilized.  This level of organization may help to order the large concentration of Prx3 units in mitochondria. 

Helices α2 and α6 are important for the R-interface. They are colored magenta.

Filament in Spacefill


Yewdall, N. A., Venugopal, H., Desfosses, A., Abrishami, V., Yosaatmadja, Y., Hampton, M. B., Gerrard, J. A., Goldstone, D. C., Mitra, A. K., and Radjainia, M.
Structures of Human Peroxiredoxin 3 Suggest Self-Chaperoning Assembly that Maintains Catalytic State.
Structure (2016) 24, 1120–1129. (PubMed)

5jcg (PDB)

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