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Disorder breathes life into a DEAD motor

Nature Structural & Molecular Biology volume 13, pages 566–569 (2006)Cite this article

SecA is an essential eubacterial protein in which the ATPase motor from DEAD-box RNA helicases has adapted to function as a processive polypeptide pump. A new report suggests that a disorder-order transition in the DEAD-box motor is responsible for distinctive thermodynamic features of SecA's conformationally coupled ATPase cycle.

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Figure 1: Structure and mechanochemistry of F1-like mechanical ATPases.
Figure 2: The DEAD-box ATPase motor in SecA and homologous helicases.
Figure 3: Possible mechanistic similarities between processive polypeptide extrusion by SecA and nucleic acid unwinding by PcrA and Vasa.

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Authors and Affiliations

  1. the Department of Biological Sciences, Columbia University, 702A Fairchild Center, New York, 10027, New York, USA

    Lorraine F Cavanaugh & John F Hunt

  2. the Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th St., New York, 10032, New York, USA

    Arthur G Palmer III

  3. the Departments of Biochemistry & Molecular Biology and Chemistry, University of Massachusetts, Lederle Graduate Research Tower 814, Amherst, 01003, Massachusetts, USA

    Lila M Gierasch

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  1. Lorraine F Cavanaugh
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  2. Arthur G Palmer III
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  3. Lila M Gierasch
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  4. John F Hunt
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Cavanaugh, L., Palmer, A., Gierasch, L. et al. Disorder breathes life into a DEAD motor. Nat Struct Mol Biol 13, 566–569 (2006). https://doi.org/10.1038/nsmb0706-566

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