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. 2017 Jan 10;112(1):109–120. doi: 10.1016/j.bpj.2016.12.010

Figure 4.

Figure 4

Conformational changes upon Neu5Ac binding. (A) Detail of the substrate-bound HiSiaP structure (PDB: 3B50 (37)), showing the Neu5Ac molecule and its interaction with the R125, E184, and H207 triade (VcSiaP numbering). (B) Superposition of the four rigid bodies of substrate-bound HiSiaP (compare Fig. 1) with substrate-free HiSiaP (PDB: 2CEY (10)). (C) Detail of the superposition in (B), showing the R125, E184, H207 triade. (D) Open/closed state (percentage) of VcSiaP mutants as determined by PELDOR spectroscopy. The PELDOR data is shown in Fig. S4. The ++/+/− indicates if 10 mM (++), 1 mM (+), or no (−) Neu5Ac was present in the experiment. The error bars represent ±3 times the SD calculated in the linear combination fitting procedure. To see this figure in color, go online.