6kkj

Crystal structure of Drug:Proton Antiporter-1 (DHA1) Family SotB, in the inward open conformation

spinqualitylabelsall models 6kkj, resolution 3.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6kkj is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.385Å Ligands: BNG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 PubMed Drug-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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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