• Institution: Max-Planck Gesellschaft MPDL
  • PNAS Streamlines Submission
  • Science Sessions: The PNAS Podcast Program

Insights into the molecular basis for substrate binding and specificity of the wild-type L-arginine/agmatine antiporter AdiC

Supporting Information

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  • Download Movie_S01 (MP4) - Visualization of potential conformational changes in AdiC involved in the release of Agm into the periplasmic space of E. coli (see also Fig. 1B). The backbone of AdiC is shown as light-blue cartoon. Selected side chains of residues involved in Agm binding, occlusion and release are displayed as sticks and color labeled: N101 (orange), M104 (green), W202 (pink), I205 (brown), E208 (blue), W293 (cyan) and S357 (violet). The substrate Agm and the identified crystallographic water molecules in the substrate-binding pocket are shown as black stick model and red balls. Water molecules appearing during the morph and binding to the substrate-binding pocket originate from the bulk solution.

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