主要促进者超家族
反转运蛋白
反转运蛋白
运输机
质子
化学
促进者
生物物理学
分子动力学
大肠杆菌蛋白质类
大肠杆菌
纳米技术
生物化学
膜
生物
材料科学
基因
物理
计算化学
法学
量子力学
政治学
作者
Qingjie Xiao,Bo Sun,Yanxia Zhou,Chen Wang,Li Guo,Jianhua He,Dong Deng
标识
DOI:10.1016/j.bbrc.2020.11.096
摘要
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.
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