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Figure 2 | BMC Structural Biology

Figure 2

From: Crystal structures from the Plasmodium peroxiredoxins: new insights into oligomerization and product binding

Figure 2

Pv Trx-Px1 and Py Trx-Px1 active sites. (A) Active sites of Pv Trx-Px1_red and Pv Trx-Px1_ox are shown in red/dark grey and orange/light grey, respectively. Note the positioning of Pro43, Thr47, and Arg125 are unchanged between the reduced and oxidized forms. The dramatic change of the active site CP in the reduced form (red) is shown as untwisting of the helix to meet the CR from its dimeric partner. As well, the formation of the disulfide results in the disruption of the final C-terminal α-helix. Note that in the reduced form the CP and CR are separated by 13.5 Å. (B) Active site of Py Trx-Px1_ox is shown for comparison.

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