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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
52
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pubmed:dateCreated |
2007-12-31
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pubmed:abstractText |
Cytoplasmic dynein is a large, microtubule-dependent molecular motor (1.2 MDa). Although the structure of dynein by itself has been characterized, its conformation in complex with microtubules is still unknown. Here, we used cryoelectron microscopy (cryo-EM) to visualize the interaction between dynein and microtubules. Most dynein molecules in the nucleotide-free state are bound to the microtubule in a defined conformation and orientation. A 3D image reconstruction revealed that dynein's head domain, formed by a ring-like arrangement of AAA+ domains, is located approximately 280 A away from the center of the microtubule. The order of the AAA+ domains in the ring was determined by using recombinant markers. Furthermore, a 3D helical image reconstruction of microtubules with a dynein's microtubule binding domain [dynein stalk (DS)] revealed that the stalk extends perpendicular to the microtubule. By combining the 3D maps of the dynein-microtubule and DS-microtubule complexes, we present a model for how dynein in the nucleotide-free state binds to microtubules and discuss models for dynein's power stroke.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-12610617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-12781660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-14704951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-14961123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-15051717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-15175652,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-15236967,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-15326307,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-15366936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-15880123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-16466743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-16585530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-16715075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-16873064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-16917055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-16946706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-17391698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-17438074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-17761194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-2954952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-4514990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-6218174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-8703926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-8742738,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18093913-9403697
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1091-6490
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
26
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pubmed:volume |
104
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20832-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:18093913-Adenosine Triphosphate,
pubmed-meshheading:18093913-Animals,
pubmed-meshheading:18093913-Cryoelectron Microscopy,
pubmed-meshheading:18093913-Cytoplasm,
pubmed-meshheading:18093913-Dictyostelium,
pubmed-meshheading:18093913-Dyneins,
pubmed-meshheading:18093913-Imaging, Three-Dimensional,
pubmed-meshheading:18093913-Microtubules,
pubmed-meshheading:18093913-Models, Biological,
pubmed-meshheading:18093913-Models, Molecular,
pubmed-meshheading:18093913-Molecular Conformation,
pubmed-meshheading:18093913-Protein Conformation,
pubmed-meshheading:18093913-Protein Structure, Tertiary,
pubmed-meshheading:18093913-Recombinant Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
Three-dimensional structure of cytoplasmic dynein bound to microtubules.
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pubmed:affiliation |
Department of Cell Biology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9039, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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