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Figure 7
XF-MS identifies conformation changes during gating of a K+ ion channel, KirBac3.1. (a) Cross-sectional view showing multiple surface-exposed and buried cavities in close KirBac3.1 (PDB-1XL4). TM1 (purple) and TM2 (green) denote transmembrane helix-1 (outer) and transmembrane helix-2 (inner), respectively. Pore helix and side helix are colored blue and red, respectively. (b) Solvent accessibility changes from the closed to the open conformation in KirBac3.1 are visualized on the structure of closed KirBac3.1, where the subunits are represented by different colors. The modified residues are shown by sticks. Color coding indicates the changes in the modification rates or solvent accessibilities upon transition from the closed to the open state. Residues that undergo increased interactions with water due to changes in the structure of the channel in the open state show dramatic increase in labeling efficiency. The results support the proposed existence of three potential gates within the channel. Results from Gupta et al. (2010BB32).

Journal logoJOURNAL OF
SYNCHROTRON
RADIATION
ISSN: 1600-5775
Volume 23| Part 5| September 2016| Pages 1056-1069
https://doi.org/10.1107/S1600577516009024
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