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![[Figure 5]](gi5041fig5mag.jpg)
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Figure 5
The C-terminal helices of AscX shift depending on the chaperone. (a) Superposition of AscX31–YscY and AscX49–LscYmeth calculated using the chaperones. AscX31 is depicted in cyan, YscY in magenta, AscX49 in green and LscY in orange. The rotation of 13° between the α2 helices was determined from the distance between the His76 residues (distance of 6.1 Å at the Cα atom) at the N-terminal end and the Glu88 residues (distance of 1.1 Å) at the C-terminal end of the helix. (b) Top view onto the C-terminal helices of AscX31 in complex with YscY. (c, d) Top view of the α2 helix in AscX49–LscYmeth and YscX50–YscY (PDB entry 7qih) aligned with AscX31–YscY. |
![[Figure 5]](gi5041fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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