Destroy and Exploit: Catalyzed Removal of Hydroperoxides from the Endoplasmic Reticulum

Figure 2

Oligomeric structure of PrxIV. (a) Upon peroxide-mediated oxidation, antiparallel PrxIV dimers are transiently linked by disulfide bonds between C_P (C¹²⁴) on one subunit and C_R (C²⁴⁵) on the other subunit (depicted in red), which is the characteristic feature of typical 2-Cys Prxs. However, dimer formation relies on hydrophobic interactions and is redox state-independent. The flexible N-terminal region (NTR) of PrxIV is oriented towards the center of the toroid-shaped, decameric complex (b). The role of the disulfide bonds linking adjacent dimers via Cys⁵¹ in the NTR (depicted in blue) is currently unclear.

(a)

(b)