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. 2011 Sep 14;286(45):39595–39605. doi: 10.1074/jbc.M111.299164

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© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 9. — Spatial relationship between Asn-93, Glu-272, and Asp-276 in XanQ permease. The figure is based on models of XanQ and selected mutants built on the structure of the UraA homolog (see Fig. 8). The modeled side chains of Asn/Ser/Thr/Gln-93 (TM3), Phe-94 (TM3), Glu-272 (TM8), Asp/Glu-276 (TM8), and Gln-324 (TM10) are displayed with PyMOL v1.4. Numbers represent minimal distances in Å between N93-E272 (oxygen-oxygen, or carbon-oxygen in N93T, or nitrogen-oxygen in N93Q), D276-E272 (oxygen-oxygen), and Q324-E272 (oxygen-oxygen). Other side chains vicinal to E272 (at distances 4.0–6.3 Å from the carboxyl oxygen atoms) are shown without labels in the bottom left panel; these are I158, L162 (TM5), L268, S269 (TM8), T320, T321, A323 (TM10), and F376 (TM12). Characteristic properties of each mutant are indicated in parenthesis (see discussion). The abbreviations are: 8-MX, high-affinity recognition of 8-methylxanthine; 8–0X, transport of uric acid (8-oxy-xanthine).