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![[Figure 6]](gi5042fig6mag.jpg)
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Figure 6
Comparison of the putative MSSM binding site in MtrRe (a, b) with the GSSG binding site from the GR–GSSG complex (PDB entry 1gra; Karplus & Schulz, 1989  ) (c, d). Coordinates for NADPH were taken from PDB entry 1grb (Karplus & Schulz, 1989). (a) and (c) show the respective disulfide substrates bound in proximity to the redox-active Cys pairs. The His–Glu ion pairs are located on opposite monomers of the dimers. In (b) and (d) the active sites are shown from a different angle in surface representation, revealing differences in the space available for substrate binding in Mtr and GR, respectively, and showing the degree of conservation of the residues lining the substrate-binding clefts as evaluated with ConSurf. Variable residues are colored turquoise and highly conserved residues are colored maroon. Cofactors, catalytic residues and substrates are represented as sticks and colored by atom type. In (e) and (f) the binding sites of Mtr and GR are overlaid, showing the increase in the size of the binding pocket that is largely due to a shift of the α3 helix in Mtr compared with GR. |
![[Figure 6]](gi5042fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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