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From Proteopedia
Crystal structure of Drug:Proton Antiporter-1 (DHA1) Family SotB, in the inward open conformation (H115A mutant)
Structural highlights
Function[SOTB_ECOLI] Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites. Transports L-arabinose and to a lesser extent IPTG. Seems to contribute to the control of the arabinose regulon. Publication Abstract from PubMedDrug-proton antiporters (DHA) play an important role in multi-drug resistance, utilizing the proton-motive force to drive the expulsion of toxic molecules, including antibiotics and drugs. DHA transporters belong to the major facilitator superfamily (MFS), members of which deliver substrates by utilizing the alternating access model of transport. However, the transport process is still elusive. Here, we report the structures of SotB, a member of DHA1 family (TCDB: 2.A.1.2) from Escherichia coli. Four crystal structures of SotB were captured in different conformations, including substrate-bound occluded, inward-facing, and inward-open states. Comparisons between the four structures reveal nonlinear rigid-body movements of alternating access during the state transition from inward-open to occluded conformation. This work not only reveals the conformational dynamics of SotB but also deepens our understanding of the alternating access mechanism of MFS transporters. Visualizing the nonlinear changes of a drug-proton antiporter from inward-open to occluded state.,Xiao Q, Sun B, Zhou Y, Wang C, Guo L, He J, Deng D Biochem Biophys Res Commun. 2021 Jan 1;534:272-278. doi:, 10.1016/j.bbrc.2020.11.096. Epub 2020 Dec 3. PMID:33280821[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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