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- Publisher Website: 10.2174/092986611796011446
- Scopus: eid_2-s2.0-79959419297
- PMID: 21529338
- WOS: WOS:000295409800002
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Article: A reporter platform for the Monitoring of in Vivo conformational changes in AcrB
Title | A reporter platform for the Monitoring of in Vivo conformational changes in AcrB |
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Authors | |
Keywords | Disulfide trapping Protein tertiary and quaternary structures |
Issue Date | 2011 |
Publisher | Bentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htm |
Citation | Protein And Peptide Letters, 2011, v. 18 n. 9, p. 863-871 How to Cite? |
Abstract | AcrB is an inner membrane protein in Escherichia coli that is a component of a triplex AcrA-AcrB-TolC (AcrAB-TolC) multidrug efflux pump. The AcrAB-TolC complex and its homologues are highly conserved among Gramnegative bacteria and are major players in conferring multidrug resistance (MDR) in many pathogens. In this study we developed a disulfide trapping method that may reveal AcrB conformational changes under the native condition in the cell membrane. Specifically, we created seven disulfide bond pairs in the periplasmic domain of AcrB, which can be used as probes to determine local conformational changes. We have developed a rigorous protocol to measure the extent of disulfide bond formation in membrane proteins under the native condition. The rigorousness of the method was verified through examining the extent of disulfide bond formation in Cys pairs separated by different distances. The blockingreducing-labeling scheme combined with fluorescence labeling made the current method convenient, reliable, and quantitative. © 2011 Bentham Science Publishers Ltd. |
Persistent Identifier | http://hdl.handle.net/10722/168535 |
ISSN | 2023 Impact Factor: 1.0 2023 SCImago Journal Rankings: 0.349 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lu, W | en_US |
dc.contributor.author | Zhong, M | en_US |
dc.contributor.author | Wei, Y | en_US |
dc.date.accessioned | 2012-10-08T03:20:13Z | - |
dc.date.available | 2012-10-08T03:20:13Z | - |
dc.date.issued | 2011 | en_US |
dc.identifier.citation | Protein And Peptide Letters, 2011, v. 18 n. 9, p. 863-871 | en_US |
dc.identifier.issn | 0929-8665 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/168535 | - |
dc.description.abstract | AcrB is an inner membrane protein in Escherichia coli that is a component of a triplex AcrA-AcrB-TolC (AcrAB-TolC) multidrug efflux pump. The AcrAB-TolC complex and its homologues are highly conserved among Gramnegative bacteria and are major players in conferring multidrug resistance (MDR) in many pathogens. In this study we developed a disulfide trapping method that may reveal AcrB conformational changes under the native condition in the cell membrane. Specifically, we created seven disulfide bond pairs in the periplasmic domain of AcrB, which can be used as probes to determine local conformational changes. We have developed a rigorous protocol to measure the extent of disulfide bond formation in membrane proteins under the native condition. The rigorousness of the method was verified through examining the extent of disulfide bond formation in Cys pairs separated by different distances. The blockingreducing-labeling scheme combined with fluorescence labeling made the current method convenient, reliable, and quantitative. © 2011 Bentham Science Publishers Ltd. | en_US |
dc.language | eng | en_US |
dc.publisher | Bentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htm | en_US |
dc.relation.ispartof | Protein and Peptide Letters | en_US |
dc.subject | Disulfide trapping | - |
dc.subject | Protein tertiary and quaternary structures | - |
dc.subject.mesh | Cysteine - Analysis | en_US |
dc.subject.mesh | Disulfides - Chemistry | en_US |
dc.subject.mesh | Drug Resistance, Multiple, Bacterial | en_US |
dc.subject.mesh | Escherichia Coli - Chemistry | en_US |
dc.subject.mesh | Escherichia Coli Proteins - Chemistry | en_US |
dc.subject.mesh | Fluorescent Dyes - Analysis | en_US |
dc.subject.mesh | Models, Molecular | en_US |
dc.subject.mesh | Multidrug Resistance-Associated Proteins - Chemistry | en_US |
dc.subject.mesh | Protein Conformation | en_US |
dc.title | A reporter platform for the Monitoring of in Vivo conformational changes in AcrB | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lu, W:luwei@hku.hk | en_US |
dc.identifier.authority | Lu, W=rp00754 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.2174/092986611796011446 | en_US |
dc.identifier.pmid | 21529338 | - |
dc.identifier.scopus | eid_2-s2.0-79959419297 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-79959419297&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 18 | en_US |
dc.identifier.issue | 9 | en_US |
dc.identifier.spage | 863 | en_US |
dc.identifier.epage | 871 | en_US |
dc.identifier.isi | WOS:000295409800002 | - |
dc.publisher.place | Netherlands | en_US |
dc.identifier.scopusauthorid | Lu, W=27868087600 | en_US |
dc.identifier.scopusauthorid | Zhong, M=36184255700 | en_US |
dc.identifier.scopusauthorid | Wei, Y=7404094290 | en_US |
dc.identifier.citeulike | 9430301 | - |
dc.identifier.issnl | 0929-8665 | - |