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. 2013 Jun 11;33(3):e00043. doi: 10.1042/BSR20130017

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© 2013 The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Licence (CC-BY)(http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.

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(a) Stereoview of the substrate analogue UDP-6N₃-GlcNAc. The electron density correspond the sigma-A weighted 2Fo–Fc map contoured at 1.0 σ. The substrate analogue is depicted with CPK colours. (b) Conformation of various nucleotide-sugars bound to representative SDR enzymes. The panel depicts CapE (this study, red); CDP-β-D-xylose bound to CDP-D-glucose 4,6-dehydratase (1wvg, yellow); GDP-rhamnose bound to GDP-mannose 4,6-dehydratase (1n7g, cyan); dTDP-D-glucose bound to dTDP-glucose 4,6-dehydratase (D128N/E129Q mutein, 1r6d, pink); and UDP-GlcNAc bound to FlaA1 (UDP-GlcNAc inverting 4,6-dehydratase, 2gn4, green). (c) Residue environment around the substrate analogue in wild-type CapE and (d) in the binding pocket of the coenzyme in K126E. Panels (c) and (d) were generated with the program LIGPLOT [51].