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![[Figure 3]](jv5013fig3mag.jpg)
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Figure 3
PPIase domain of CrTIG1ΔRBD. (a) Secondary-structure elements are presented as ribbons. The loops are named according to the FKBP fold (Lücke & Weiwad, 2011  ). Conserved key residues involved in PPIase activity are shown as sticks. (b) Electrostatic surface potential (top) and hydrophobicity plot of the PPIase domain alone. The electrostatic surface potential was calculated with the APBS plugin from PyMOL. Red indicates negative charge and blue indicates positive charge. The hydrophobicity plot was generated with the color_h Python script in PyMOL (where red indicates the highest hydrophobicity; Eisenberg et al., 1984). (c) Structural alignment of the PPIase domain of CrTIG1ΔRBD (red) with those of EcTF (beige; PDB entry 1w26; Ferbitz et al., 2004) and the FKBP13–FK506 complex (light blue; PDB entry 4nnr; Schultz et al., 1994). (d) Hydrogen bonds between the loops in the PPIase domain and arm 1 of the C-terminal domain (SBD). (e) Hydrogen bonds between the loops in the PPIase domain and the preceding linker helix. |
![[Figure 3]](jv5013fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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