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. 2008 Nov 6;105(45):17390–17395. doi: 10.1073/pnas.0805027105

Fig. 6.

Fig. 6.

Changes of the active site structure upon proteolytic activation of EcPOX. (A) Superposition of the active sites of full-length EcPOX (green) and EcPOXΔ23 (yellow). Amino acids contributed from the neighboring subunit are labeled with an apostrophe. Note the position of F465 in EcPOXΔ23, which adopts a conformation identical to that of F479 in LpPOX. (B) Illustration of the structural transition of the C-terminal linker region (residues 531–549) and an active center loop harboring F465 upon proteolytic activation. The full-length enzyme is shown in green and EcPOXΔ23 is shown in yellow. Residues Y549 and F465 are highlighted.