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Figure 1
Event map generated by PanDDA around Tyr110 and fragments 1 and 2. (a) Architecture of the apo BpsDsbA structure (PDB entry 4k2d; Ireland et al., 2014BB23) represented as a cartoon. α-Helices and β-strands are numbered α1–α7 and β1–β5, respectively. The active-site cysteines are indicated by yellow spheres; Tyr110 is represented in blue in stick format. (b) Close-up of the orientation of Tyr110 in the apo structure (no ligand present) and (c) and (d) in the presence of 1 and 2, respectively. The Tyr110 side chain rotates to the right in this orientation (viewed along the Cβ—Cγ bond) towards helix α3 compared with the apo structure. This shift opens a small hydrophobic pocket into which the fragment binds. The reference apo 2mFoDFc map, contoured at 1 r.m.s.d. and shown in orange, is the result of averaging 32 electron-density maps of apo BpsDsbA. The PanDDA event maps are shown in blue and are contoured at 2 r.m.s.d. for 1 and 2 in (c) and (d), respectively. These maps are estimates of the ligand-bound state (Pearce, Krojer, Bradley et al., 2017BB41). The background density correction (BDC) and the resolution (Res) are given for the event maps in (c) and (d).

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
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