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. 2016 Apr 18;7:11337. doi: 10.1038/ncomms11337

Figure 4. Structural differences between Mep2 and bacterial ammonium transporters.

Figure 4

(a) ICL1 in AfAmt-1 (light blue) and CaMep2 (dark blue), showing unwinding and inward movement in the fungal protein. (b) Stereo diagram viewed from the cytosol of ICL1, ICL3 (green) and the CTR (red) in AfAmt-1 (light colours) and CaMep2 (dark colours). The side chains of residues in the RxK motif as well as those of Tyr49 and His342 are labelled. The numbering is for CaMep2. (c) Conserved residues in ICL1-3 and the CTR. Views from the cytosol for CaMep2 (left) and AfAmt-1, highlighting the large differences in conformation of the conserved residues in ICL1 (RxK motif; blue), ICL2 (ER motif; cyan), ICL3 (green) and the CTR (red). The labelled residues are analogous within both structures. In b and c, the centre of the trimer is at top.