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. 2012 Feb 10;287(14):10780–10790. doi: 10.1074/jbc.M111.322974

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© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 3. — Binding mode of UDP-Galp in arginine mutants. A, superposition of R327A AfUGM with bound UDP-Galp (blue) on reduced AfUGM·UDP-Galp (red). UDP-Galp is bound in a non-productive binding mode in R327A AfUGM. Arg-182 is in the same position as in wild type AfUGM. B, the R182K AfUGM mutant with bound UDP-Galp. Only the UDP moiety is visible and no density for Galp moiety. R182K is within 3.6 Å from the Asn-457 side chain but has no interaction with the phosphates or the galactose moiety. Phe-66 points out of the active site. C, R327K AfUGM with bound UDP-Galp. NZ of R327K is in the same position as NH1 of Arg-327 and makes the same interactions with galactose moiety and the β-phosphate as in wild type complex. Phe-66 points into active site.