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. 2021 May 25;40(14):e107294. doi: 10.15252/embj.2020107294

Figure 1. Overall structure and functional characterization of KCC3b‐PM and KCC1Δ19.

Figure 1

  • A
    Density map of KCC1Δ19, coloured by protomer. ATP bound to the CTD is represented as spheres.
  • B
    Density map of KCC3b‐PM, coloured by protomer, with N‐terminal region highlighted in bright red.
  • C, D
    Rb+ uptake activity of WT and mutant constructs for KCC1 (C) and KCC3b (D) under isotonic (dark grey bars) and hypotonic conditions (light grey bars). Values are mean (± SE) background‐subtracted transport rates of 10 oocytes from 3 to 6 experiments in the presence (indicated by +Fu) or absence of 1.5 mM furosemide.
  • E–G
    CTD arrangement of KCC1 (construct Δ19) (E, F) and KCC3b (construct PM: S45D/T940D/T997D, panel G). Of the TMD, only TM helices 11 and 12 are shown for clarity. Cα distances (in Å) between marker atoms S634 (KCC1) and S648 (KCC3b) are indicated by a black line.
  • H
    Hinge region (red ribbon representation) for conformational change between state A and B of KCC1 predicted by DynDom (Lee et␣al, 2003).