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![[Figure 3]](gi5042fig3mag.jpg)
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Figure 3
(a) Structural alignment of MtrRe and the homologous oxidoreductases GR (PDB entries 1gra and 1grb; Karplus & Schulz, 1989  ; NADPH from the latter), DLD (PDB entry 2eq9; T. Nakai & N. Kamiya, unpublished work) and MerA (PDB entries 1zk7 and 4k7z; Ledwidge et al., 2005; A. Dong, M. Falkowski, M. Malone, S. M. Miller & E. F. Pai, unpublished work; NADPH from the latter). Cofactors and the redox-active Cys pairs are represented as sticks and colored by atom type. (b) Overlay of MtrRe and GR (PDB entries 1gra and 1grb) showing the arginines stabilizing the 2′ phosphate group of NADPH, and Phe178 in Mtr corresponding to Tyr197 in GR which undergoes conformational change when NADPH binds. |
![[Figure 3]](gi5042fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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