NDLI: The structure of the myosin VI motor reveals the mechanism of directionality reversal

Content Provider	PubMed Central
Author	Julie, Ménétrey Bahloul, Amel Wells, Amber Yengo, Christopher Morris, Carl Sweeney, H. Lee Anne, Houdusse
Abstract	We have solved a 2.4Å structure of a truncated version of the reverse direction myosin motor, myosin VI, that contains the motor domain and binding sites for two calmodulins. The structure reveals only minor differences in the motor domain as compared to plus-end directed myosins, with the exception of two unique inserts. The first insert is near the nucleotide-binding pocket, and alters the rates of nucleotide association and dissociation. The second unique insert forms an integral part of the myosin VI converter domain along with a calmodulin bound to a previously unseen binding motif within the insert. This serves to redirect the effective “lever arm” of myosin VI, which includes a second calmodulin bound to an “IQ motif,” towards the pointed (−) end of the actin filament. This repositioning largely accounts for the reverse directionality of this class of myosin motors. We propose a model incorporating a kinesin-like uncoupling/docking mechanism to fully explain the movements of myosin VI.
Related Links	http://dx.doi.org/10.1038/nature03592
Ending Page	785
Page Count	7
Starting Page	779
File Format	PDF
ISSN	00280836
e-ISSN	14764687
Journal	Nature
Issue Number	7043
Volume Number	435
Language	English
Publisher Date	2005-06-09
Access Restriction	Open
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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