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Figure 3
(a) Structure-based sequence alignment of Grxs (refer to Table 2[link] for PDB codes and organism information). Identical, conserved and semi-conserved residues are marked with asterisks, colons and dots, respectively. The active-site residues (CXXC for dithiol Grx and CXXS for monothiol Grx) and atoms involved in interactions with Gly, Cys and γGlu of GSH are highlighted in blue, orange and red, and green, respectively. (b) A superposition of Cα atoms of Grxs is shown. Apart from insertion regions, the largest deviations are observed in the α1, α3 and α5 helices. Identical, conserved, semi-conserved and weakly conserved residues are rendered in red, pink, grey and blue, respectively. (c) Comparison of GSH-binding site motifs in Grxs. Positions of conserved CXXC/CXXS (cyan), TVP (yellow), CDD (green) motifs and Lys26 (orange) and Gln/Arg63 (blue) residues are highlighted. The conserved Gly-Gly doublet is also marked. Bound GSH molecules (pink) are shown as ball-and-stick models.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
Volume 70| Part 1| December 2014| Pages 91-100
doi:10.1107/S1399004713025285
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