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. Author manuscript; available in PMC: 2017 Oct 4.
Published in final edited form as: Structure. 2016 Sep 1;24(10):1668–1678. doi: 10.1016/j.str.2016.07.012

Figure 3.

Figure 3

Fully Folded and Locally Unfolded Conformations of XcPrxQ. A. The active FF conformation (left) and the LU disulfide conformation are shown (right) as cartoons colored by local mobility as indicated by B-factor, and with sticks for CP, CR and the conserved active site Pro, Thr and Arg. The largest conformation changes involve the helix 3 region that is highlighted in yellow. This structural rearrangement moves CP away from the active site pocket, disrupting all of its hydrogen bonding interactions, as described by Liao et al. (Liao et al., 2009). B. The active site of the XcPrxQ FF structure with 2FO-FC density (thin blue mesh 1.5 ρrms pink mesh 3.5 ρrms). C. Same as B but for the LU CP-CR disulfide structure.