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Fig. 6 | BMC Biology

Fig. 6

From: High-resolution structure of the amino acid transporter AdiC reveals insights into the role of water molecules and networks in oligomerization and substrate binding

Fig. 6

Contribution of water in AdiC dimer stabilization. A On the left, the overall structure of AdiC is shown as viewed from the periplasmic side. The small box indicates the location of the cavity at the dimer interface and is displayed enlarged in the right box. All possible hydrogen bond interactions ≤ 3.4 Å are shown as dashed lines and distances are given in Å. The AdiC dimer (transparent ribbons), amino acid side chains involved in water-mediated interface stabilization (sticks), and the labels are colored according to the individual monomeric color code (blue and yellow color hues) as in Fig. 1. Water molecules (a–d) are displayed as red spheres. B Comparison of the melting temperature (Tm) of AdiC-wt and three point mutants (AdiC-Q88E, AdiC-Y367F, AdiC-T421V). The determined Tm values are from at least three independent experiments, each in duplicates. Error bars represent SEM. If not visible, error bars are smaller than symbols

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BMC Biology

ISSN: 1741-7007

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