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![[Figure 8]](wa5133fig8mag.jpg)
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Figure 8
Comparison of the protomers of CcScsC C2S, PmScsC (extended), StScsC and EcDsbA. (a) Superimposition of the globular domains of the four oxidoreductases shows the structural conservation between these proteins: EcDsbA (PDB entry 1fvk; Guddat et al., 1997  ) in light pink, StScsC (PDB entry 4gxz; Shepherd et al., 2013) in grey, PmScsC (PDB entry 5id4; Furlong et al., 2017) in cyan and CcScsC (PDB entry 7rgv) in green. In each case, the CXXC and cis-proline loop residues are shown as pink sticks. (b) The same structures are displayed side by side showing the α-helix/loop difference in the globular domains (arrow). The sequence identified to be responsible for the flexible, dynamic nature of PmScsC is highlighted in red. The homologous region of CcScsC is also coloured red. |
![[Figure 8]](wa5133fig8.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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