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Concluding Remarks

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Mechanism of Functional Expression of F1-ATPase

Part of the book series: SpringerBriefs in Molecular Science ((BRIEFSMOLECULAR))

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Abstract

AcrB, a homotrimer possessing a triangular-prism shape, is the principal part of the AcrA–AcrB–TolC complex which extrudes a variety of drugs from a cell. AcrB comprises three protomers which are in access (A), binding (B), and extrusion (E) states along a drug-transport cycle, respectively. According to a suggestion made in the literature, the three protomers exhibit a sequential conformational change expressed as (A, B, E)→(B, E, A)→(E, A, B)→(A, B, E). This change, which is referred to as the “functional rotation”, is achieved with the use of the so-called proton motive force yielding repeated proton binding to and dissociation from AcrB. In this chapter, we point out that F1-ATPase considered in Chap. 3 and AcrB share physically the same rotation mechanism. Whenever the structure of one of the three portions forming a protein complex is perturbed in the direction that a solvent-entropy loss is caused, the structures of the other two portions are reorganized to make up for the loss. We also comment on the rotation mechanism of V1-ATPase which we intend to explore in the next stage.

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Authors and Affiliations

  1. Institute of Advanced Energy, Kyoto University, Uji, Kyoto, Japan

    Masahiro Kinoshita

  2. Graduate School of Science, Chiba University, Chiba, Japan

    Masahiro Kinoshita

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  1. Masahiro Kinoshita
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Kinoshita, M. (2021). Concluding Remarks. In: Mechanism of Functional Expression of F1-ATPase. SpringerBriefs in Molecular Science. Springer, Singapore. https://doi.org/10.1007/978-981-33-6232-1_4

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