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Figure 4
(a, b) Stereopairs of ensemble superposition for the NMR solution structures of the Br. melitensis (a) and Ba. henselae (b) glutaredoxins. The conserved pair of active-site cysteine side chains are drawn in gray and yellow. (c) The lowest energy conformer from (a) rotated to show the angle of SSH relative to the β-sheet surface. (d) The lowest energy conformer from (b) with a more parallel SSH angle. (e) The human glutaredoxin 1 structure with the extra N-terminal helix (blue) and the HSL/SSH region (red trapezoid) indicated. (f) The E. coli glutaredoxin 3 structure. (g) Close-up view of the convergent superposition of the CPYC active-site region (left) juxtaposed with the divergent and non-overlapping structures for the HSL/SSH regions. Only the region near the active site and the HSL/SSH regions are colored according to the above figures, while the remainder of the proteins are drawn in white.

ISSN: 2053-230X
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