Nature Structural & Molecular Biology 13, 566 - 569 (2006)
doi:10.1038/nsmb0706-566
Disorder breathes life into a DEAD motorLorraine F Cavanaugh1, Arthur G Palmer III2, Lila M Gierasch3
& John F Hunt11
Lorraine F. Cavanaugh and John F. Hunt are in the Department of Biological Sciences, 702A Fairchild Center, Columbia University, New York, New York 10027, USA jfhunt@biology.columbia.edu
2
Arthur G. Palmer III is in the Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th St., New York, New York 10032, USA
3
Lila M. Gierasch is in the Departments of Biochemistry & Molecular Biology and Chemistry, Lederle Graduate Research Tower 814, University of Massachusetts, Amherst, Massachusetts 01003, USA. 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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