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![[Figure 4]](jb5056fig4mag.jpg)
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Figure 4
Comparison of the TrxR–Trx complex in E. coli with two fragment clusters at the Trx site in Msm-TrxR. (a) X-ray structure (PDB entry 1f6m; Lennon et al., 2000  ) showing Trx interacting with the FR conformation of E. coli TrxR (gray, NADPH-binding domain; blue, FAD-binding domain; purple, Trx). The Trx loop (Tyr70–Ile75; purple) interacts with a binding cleft in the NADPH-binding domain (gray) in the FR conformation. (b) Fragments (orange) bound at the Trx interaction site can be separated into two clusters and interact with both domains and protomers (shades of gray, NADPH-binding domain; shades of blue, FAD-binding domain). Hydrogen bonds are shown as black dashed lines. |
![[Figure 4]](jb5056fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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