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. Author manuscript; available in PMC: 2021 Jun 1.
Published in final edited form as: Plant J. 2020 Apr 18;102(6):1107–1126. doi: 10.1111/tpj.14745

Figure 2.

Figure 2.

(A) Each LCI1 subunit forms a channel (colored green) that spans approximately two-thirds of the transmembrane. The radius of the channel was calculated using the program HOLE (Smart et al., 1993). The channel is closed due to interaction between the sidechains of residues E87 and N161. (B) The LCI1 channel (colored pink) is surrounded by 22 amino acids, including V26, A30, L33, L42, Y52, Y56, F60, I66, F77, Q80, I83, I84, N125, A128, T137, V141, F142, I147, A150, L154 and V157, and containing a potential CO2-binding site located right below residues E87 and N161. This channel representation was generated using the program CAVER (http://loschmidt.chemi.muni.cz/caver). The secondary structural elements of the LCI1 protomer are in gray, and residues involved in forming this channel, along with residues E87 and N161, are represented by green sticks.