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-Structure paper
タイトル | In situ structure of the AcrAB-TolC efflux pump at subnanometer resolution. |
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ジャーナル・号・ページ | Structure, Vol. 30, Issue 1, Page 107-113.e3, Year 2022 |
掲載日 | 2022年1月6日 |
著者 | Muyuan Chen / Xiaodong Shi / Zhili Yu / Guizhen Fan / Irina I Serysheva / Matthew L Baker / Ben F Luisi / Steven J Ludtke / Zhao Wang / |
PubMed 要旨 | The tripartite AcrAB-TolC assembly, which spans both the inner and outer membranes in Gram-negative bacteria, is an efflux pump that contributes to multidrug resistance. Here, we present the in situ ...The tripartite AcrAB-TolC assembly, which spans both the inner and outer membranes in Gram-negative bacteria, is an efflux pump that contributes to multidrug resistance. Here, we present the in situ structure of full-length Escherichia coli AcrAB-TolC determined at 7 Å resolution by electron cryo-tomography. The TolC channel penetrates the outer membrane bilayer through to the outer leaflet and exhibits two different configurations that differ by a 60° rotation relative to the AcrB position in the pump assembly. AcrA protomers interact directly with the inner membrane and with AcrB via an interface located in proximity to the AcrB ligand-binding pocket. Our structural analysis suggests that these AcrA-bridged interactions underlie an allosteric mechanism for transmitting drug-evoked signals from AcrB to the TolC channel within the pump. Our study demonstrates the power of in situ electron cryo-tomography, which permits critical insights into the function of bacterial efflux pumps. |
リンク | Structure / PubMed:34506732 / PubMed Central |
手法 | EM (サブトモグラム平均) |
解像度 | 7.0 Å |
構造データ | EMDB-24609: Subnanometer in situ structure of the AcrAB-TolC efflux pump bound with MBX |
由来 |
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