Li-Wei Hung, Heung-Bok Kim, Satoshi Murakami, Goutam Gupta, Chang-Yub Kim, Thomas C Terwilliger
{"title":"3.5 Å分辨率下AcrB与利奈唑胺络合的晶体结构。","authors":"Li-Wei Hung, Heung-Bok Kim, Satoshi Murakami, Goutam Gupta, Chang-Yub Kim, Thomas C Terwilliger","doi":"10.1007/s10969-013-9154-x","DOIUrl":null,"url":null,"abstract":"<p><p>AcrB is an inner membrane resistance-nodulation-cell division efflux pump and is part of the AcrAB-TolC tripartite efflux system. We have determined the crystal structure of AcrB with bound Linezolid at a resolution of 3.5 Å. The structure shows that Linezolid binds to the A385/F386 loops of the symmetric trimer of AcrB. A conformational change of a loop in the bottom of the periplasmic cleft is also observed.</p>","PeriodicalId":73957,"journal":{"name":"Journal of structural and functional genomics","volume":"14 2","pages":"71-5"},"PeriodicalIF":0.0000,"publicationDate":"2013-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s10969-013-9154-x","citationCount":"38","resultStr":"{\"title\":\"Crystal structure of AcrB complexed with linezolid at 3.5 Å resolution.\",\"authors\":\"Li-Wei Hung, Heung-Bok Kim, Satoshi Murakami, Goutam Gupta, Chang-Yub Kim, Thomas C Terwilliger\",\"doi\":\"10.1007/s10969-013-9154-x\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>AcrB is an inner membrane resistance-nodulation-cell division efflux pump and is part of the AcrAB-TolC tripartite efflux system. We have determined the crystal structure of AcrB with bound Linezolid at a resolution of 3.5 Å. The structure shows that Linezolid binds to the A385/F386 loops of the symmetric trimer of AcrB. A conformational change of a loop in the bottom of the periplasmic cleft is also observed.</p>\",\"PeriodicalId\":73957,\"journal\":{\"name\":\"Journal of structural and functional genomics\",\"volume\":\"14 2\",\"pages\":\"71-5\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2013-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1007/s10969-013-9154-x\",\"citationCount\":\"38\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of structural and functional genomics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1007/s10969-013-9154-x\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of structural and functional genomics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/s10969-013-9154-x","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Crystal structure of AcrB complexed with linezolid at 3.5 Å resolution.
AcrB is an inner membrane resistance-nodulation-cell division efflux pump and is part of the AcrAB-TolC tripartite efflux system. We have determined the crystal structure of AcrB with bound Linezolid at a resolution of 3.5 Å. The structure shows that Linezolid binds to the A385/F386 loops of the symmetric trimer of AcrB. A conformational change of a loop in the bottom of the periplasmic cleft is also observed.