Fig. 5: Ι Effect of the protonation state of E207 on structural changes in the occluded conformation of PfCRTDd2. | Nature Communications

Fig. 5: Ι Effect of the protonation state of E207 on structural changes in the occluded conformation of PfCRTDd2.

From: pH-dependence of the Plasmodium falciparum chloroquine resistance transporter is linked to the transport cycle

Fig. 5

a Distance between hydrogen bond donors and acceptors, E207 and E372/K80/N84, in one MD simulation of the occluded conformation of PfCRTDd2, with E207 deprotonated. Dotted line indicates the threshold distance of 3.5 Å for the formation of a hydrogen bond. b Snapshot from one MD simulation illustrating the hydrogen bonds between E207 and K80 and N84 in the occluded conformation, with E207 deprotonated. c Distance between hydrogen bond donors and acceptors, E207 and E372/K80/N84, in one MD simulation of the occluded conformation of PfCRT, with E207 protonated. d Snapshot from one MD simulation illustrating hydrogen bond formation between E207 and E372 in the occluded conformation, with E207 protonated. Source data are provided as a Source Data file86.

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