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![[Figure 1]](lp5062fig1mag.jpg)
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Figure 1
Secondary structure and topology of RBP and its permuted halves. (a) Secondary-structure alignment with the amino-acid sequence of RBP. Secondary-structure annotations derived from PDBsum (Laskowski et al., 2018  ) are colored salmon for RBP, blue for RBP-CPN and yellow for RBP-CPC. β-Sheets are sequentially labeled with letters in the order of the sequence and α-helices are labeled with numbers. These labels correspond to the topology representation (b, c, d) adapted from Fukami-Kobayashi et al. (1999), where β-sheets are depicted as triangles and α-helices as circles. The arrangement of the secondary-structure elements reflects their three-dimensional order for RBP (b), RBP-CPC (c) and RBP-CPN (d). The N- and C-termini are labeled N and C, respectively, and the connections between the secondary-structure elements are shown as arrows. The connections of the two possible configurations of β-strand I, either to α-helix 8 or β-strand J′, in RBP-CPC are shown as dotted arrows as these stretches are not resolved in the crystal structure. |
![[Figure 1]](lp5062fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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