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Structure of human cytoplasmic dynein-2 primed for its power stroke

Schmidt, Helgo ; Zalyte, Ruta ; Urnavicius, Linas ; Carter, Andrew P

Nature (London), 2015-02, Vol.518 (7539), p.435-438 [Periódico revisado por pares]

England: Nature Publishing Group

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Título:
Structure of human cytoplasmic dynein-2 primed for its power stroke
Autor: Schmidt, Helgo ; Zalyte, Ruta ; Urnavicius, Linas ; Carter, Andrew P
Assuntos: Adenosine Diphosphate - analogs & derivatives ; Adenosine Diphosphate - metabolism ; Binding Sites ; Cell research ; Cellular biology ; Cellular control mechanisms ; Crystallography, X-Ray ; Cytoplasm ; Cytoplasmic Dyneins - chemistry ; Cytoplasmic Dyneins - metabolism ; Dynein ; Humans ; Hydrolysis ; Models, Molecular ; Movement ; Physiological aspects ; Protein Conformation
É parte de: Nature (London), 2015-02, Vol.518 (7539), p.435-438
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: Members of the dynein family, consisting of cytoplasmic and axonemal isoforms, are motors that move towards the minus ends of microtubules. Cytoplasmic dynein-1 (dynein-1) plays roles in mitosis and cellular cargo transport, and is implicated in viral infections and neurodegenerative diseases. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Here we present the crystal structure of the human cytoplasmic dynein-2 motor bound to the ATP-hydrolysis transition state analogue ADP.vanadate. The structure reveals a closure of the motor's ring of six AAA+ domains (ATPases associated with various cellular activites: AAA1-AAA6). This induces a steric clash with the linker, the key element for the generation of movement, driving it into a conformation that is primed to produce force. Ring closure also changes the interface between the stalk and buttress coiled-coil extensions of the motor domain. This drives helix sliding in the stalk which causes the microtubule binding domain at its tip to release from the microtubule. Our structure answers the key questions of how ATP hydrolysis leads to linker remodelling and microtubule affinity regulation.
Editor: England: Nature Publishing Group
Idioma: Inglês

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Structure of human cytoplasmic dynein-2 primed for its power stroke

Schmidt, Helgo ; Zalyte, Ruta ; Urnavicius, Linas ; Carter, Andrew P

England: Nature Publishing Group

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