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. Author manuscript; available in PMC: 2014 Aug 22.
Published in final edited form as: Chem Biol. 2013 Jul 25;20(8):991–1001. doi: 10.1016/j.chembiol.2013.06.011

Figure 5. Crystal structure of AcePrx-1.

Figure 5

A. Crystals of AcePrx-1 are colorless in the absence of conoidin A.

B. AcePrx-1 crystals grown in the presence of conoidin A are yellow, suggesting that conoidin A binds to the enzyme.

C. AcePrx-1 adopts a fold similar to other peroxiredoxins. The most similar structure is human Prx-4 (PDB code 3TJB). AcePrx-1 forms dimers principally via inter-strand contacts to form an eight-stranded β-sheet. Dashed lines connect the active site cysteines across the dimer interface.

D. Five AcePrx-1 dimers assemble into a decamer in solution and in the crystal structure. See also Figure S2.