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![[Figure 1]](jb5056fig1mag.jpg)
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Figure 1
Conformational change of a bacterial TrxR during catalysis. The TrxR can be separated into a NADPH-binding domain (gray) with the cofactor NADPH (green) and a FAD-binding domain (blue) with bound FAD (gold). Prokaryotic TrxR is dependent on a conformational change in which the FAD-binding domain rotates around the NADPH-binding domain, leading to the reduced active site (yellow) being exposed to the surface for interaction with Trx (purple): left, FO (PDB entry 1tde; Waksman et al., 1994  ); right, FR (PDB entry 1f6m; Lennon et al., 2000). Both proteins of the TrxR–Trx complex have one cysteine of the active site mutated to a serine, leading to the formation of a covalently linked disulfide between TrxR and Trx (Waksman et al., 1994; Lennon et al., 2000). |
![[Figure 1]](jb5056fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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