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- Robert Schulz
- School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany
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- Attilio V. Vargiu
- Dipartimento di Fisica, Università di Cagliari, S.P. Monserrato-Sestu km 0.7, 09042 Monserrato, Italy
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- Paolo Ruggerone
- Dipartimento di Fisica, Università di Cagliari, S.P. Monserrato-Sestu km 0.7, 09042 Monserrato, Italy
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- Ulrich Kleinekathöfer
- School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany
書誌事項
- 公開日
- 2015
- 権利情報
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- http://creativecommons.org/licenses/by/3.0/
- DOI
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- 10.1155/2015/487298
- 公開者
- Wiley
この論文をさがす
説明
<jats:p>As active part of the major efflux system in<jats:italic>E. coli</jats:italic>bacteria, AcrB is responsible for the uptake and pumping of toxic substrates from the periplasm toward the extracellular space. In combination with the channel protein TolC and membrane fusion protein AcrA, this efflux pump is able to help the bacterium to survive different kinds of noxious compounds. With the present study we intend to enhance the understanding of the interactions between the domains and monomers, for example, the transduction of mechanical energy from the transmembrane domain into the porter domain, correlated motions of different subdomains within monomers, and cooperative effects between monomers. To this end, targeted molecular dynamics simulations have been employed either steering the whole protein complex or specific parts thereof. By forcing only parts of the complex towards specific conformational states, the risk for transient artificial conformations during the simulations is reduced. Distinct cooperative effects between the monomers in AcrB have been observed. Possible allosteric couplings have been identified providing microscopic insights that might be exploited to design more efficient inhibitors of efflux systems.</jats:p>
収録刊行物
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- BioMed Research International
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BioMed Research International 2015 1-12, 2015
Wiley