X-ray structure of a functional full-length dynein motor domain
Takahide Kon, Kazuo Sutoh & Genji Kurisu
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Nature Structural & Molecular Biology 18, 638–642 (2011)
doi:10.1038/nsmb.2074
Received 16 February 2011 Accepted 27 April 2011
Published online 22 May 2011
Abstract
Dyneins are large microtubule-based motors that power a wide variety of cellular processes. Here we report a 4.5-Å X-ray crystallographic analysis of the entire functional motor domain of cytoplasmic dynein with ADP from Dictyostelium discoideum, which has revealed the detailed architecture of the functional units required for motor activity, including the ATP-hydrolyzing ring, the long coiled-coil microtubule-binding stalk and the force-generating rod-like linker. We discovered a Y-shaped protrusion composed of two long coiled coils—the stalk and the newly identified 'strut'. This structure supports our model in which the strut coiled coil actively contributes to communication between the primary ATPase site in the ring and the microtubule-binding site at the tip of the stalk coiled coil. Our work also provides insight into how the two motor domains are arranged and how they interact with each other in a functional dimer form of cytoplasmic dynein.
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NOTA DESTE BLOGGER:
Reparem a linguagem teleológica no abstract. E ainda têm a cara de pau de dizer que Darwin eliminou a teleologia de uma vez por todas em biologia. Nada mais falso!!!
