Article abstract
Nature Structural & Molecular Biology 15, 591 - 597 (2008)
Published online: 30 May 2008 | doi:10.1038/nsmb.1429
Long single 
-helical tail domains bridge the gap between structure and function of myosin VI
Benjamin J Spink1, Sivaraj Sivaramakrishnan1, Jan Lipfert2,4, Sebastian Doniach2,3 & James A Spudich1
Abstract
Myosin VI has challenged the lever arm hypothesis of myosin movement because of its ability to take 
36-nm steps along actin with a canonical lever arm that seems to be too short to allow such large steps. Here we demonstrate that the large step of dimeric myosin VI is primarily made possible by a medial tail in each monomer that forms a rare single 
-helix of 10 nm, which is anchored to the calmodulin-bound IQ domain by a globular proximal tail. With the medial tail contributing to the 36-nm step, rather than dimerizing as previously proposed, we show that the cargo binding domain is the dimerization interface. Furthermore, the cargo binding domain seems to be folded back in the presence of the catalytic head, constituting a potential regulatory mechanism that inhibits dimerization.
- Department of Biochemistry, Stanford University, 279 Campus Drive, Stanford, California 94305, USA.
- Department of Physics, 382 Via Pueblo Mall, Stanford University, Stanford, California 94305, USA
- Department of Applied Physics, 382 Via Pueblo Mall, Stanford University, Stanford, California 94305, USA.
- Present address: Kavli Institute of Nanoscience, Faculty of Applied Sciences, Delft University of Technology, 2628 CJ Delft, The Netherlands.
Correspondence to: James A Spudich1 e-mail: jspudich@stanford.edu
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