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. 2016 Apr 26;7(2):e00492-16. doi: 10.1128/mBio.00492-16

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Copyright © 2016 Tonthat et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.

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FIG 5 — A. fumigatus FKBP12(V91C) mutation captures the intermolecular contact. (A) SDS-PAGE purification of FKBP12(V91C) from both SHuffle and C41(DE3) cells. Dimers are evident in the gel run without a reducing agent. Addition of a reducing agent leads to reduction of the disulfide bond and the proteins running as monomers. (B) Crystal structure of A. fumigatus FKBP12(V91C). (C) 2F_o-F_c electron density map contoured at 1 σ showing the region around the V91C disulfide bond and the Pro89-Pro90 bond, which adopts a twisted, trans conformation-like state. (D) Ribbon diagram showing a closeup of the Pro89-Pro90 region with the residues labeled. Note that the green-labeled Pro90 side chains appear distorted.