Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 186, Issue 3, Pages 367-375Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2014.03.019
Keywords
Microtubule; Cytoskeleton; Motor protein; Dynein; ATPases Associated with diverse cellular; Activities (AAA plus ); Coiled-coil
Funding
- Medical Research Council, UK [MC_UP_A025_1011 (AC)]
- MRC [MC_UP_A025_1011] Funding Source: UKRI
- Medical Research Council [MC_UP_A025_1011] Funding Source: researchfish
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Dyneins are large protein complexes that act as microtubule based molecular motors. The dynein heavy chain contains a motor domain which is a member of the AAA+ protein family (ATPases Associated with diverse cellular Activities). Proteins of the AAA+ family show a diverse range of functionalities, but share a related core AAA+ domain, which often assembles into hexameric rings. Dynein is unusual because it has all six AAA+ domains linked together, in one long polypeptide. The dynein motor domain generates movement by coupling ATP driven conformational changes in the AAA+ ring to the swing of a motile element called the linker. Dynein binds to its microtubule track via a long antiparallel coiled-coil stalk that emanates from the AAA+ ring. Recently the first high resolution structures of the dynein motor domain were published. Here we provide a detailed structural analysis of the six AAA+ domains using our Saccharomyces cerevisiae crystal structure. We describe how structural similarities in the dynein AAA+ domains suggest they share a common evolutionary origin. We analyse how the different AAA+ domains have diverged from each other. We discuss how this is related to the function of dynein as a motor protein and how the AAA+ domains of dynein compare to those of other AAA+ proteins. (C) 2014 The Authors. Published by Elsevier Inc.
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