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. 1999 Oct 26;96(22):12333–12338. doi: 10.1073/pnas.96.22.12333

Figure 1.

Figure 1

Overall structure and secondary structural elements of HBP23. (A) A ribbon representation of HBP23 showing the secondary structural elements. The α-helices in light blue and β-strands in pale pink form a thioredoxin fold. The other α-helices and β-strands are shown in blue and purple, respectively. The side chains of Cys-52 and Cys-173 are shown with ball-and-stick models. (B) A view along the 2-fold axis of the ribbon representation of the HBP23 dimer. The secondary structural elements of Molecule A are shown in red (α-helices) and pale pink (β-strands) and those of Molecule B in blue (α-helices) and sky blue (β-strands). Loop regions of Molecule B are in dark gray. The side chains of two cysteine residues (Cys-52 and Cys-173) at the active site are indicated by ball-and-stick models. (C) The secondary structure elements and sequence alignment of HBP23 and the related Prxs. The secondary structural elements of HBP23 and ORF6 are shown (Top and Bottom, respectively), with the same color codes as in A. For the homologues of 2-Cys Prxs (PAG, natural killer cell-enhancing factor A, and mouse macrophage stress protein), substituted residues are shown. Identical residues between HBP23 and ORF6 are highlighted in yellow.