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Substrate-induced unfolding of protein disulfide isomerase displaces the cholera toxin A1 subunit from its holotoxin.

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Academic year: 2017

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Figure 1. Loss of PDI structure in the presence of CTA1. Far-UV CD spectra of PDI (green), CTA1 (blue), and both proteins in the same sample at a 1:1 molar ratio (red) are shown
Figure 2. Structure of PDI in the absence or presence of CTA1. Curve fitting (left panels) and second derivatives (right panels) for the FTIR spectrum of PDI recorded in the absence (A, C, E, G) or presence (B, D, F, H) of 13 C-labeled CTA1 are shown
Figure 3. Refolding of disordered PDI. PDI was placed at 10uC in sodium borate buffer (pH 7.0) containing 13 C-labeled CTA1 and 1 mM GSH
Figure 8. ERp57 and ERp72 do not disassemble the CT holotoxin and do not unfold upon contact with CTA1

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