Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
49
pubmed:dateCreated
2006-12-6
pubmed:databankReference
pubmed:abstractText
Intracellular active transport is driven by ATP-hydrolyzing motor proteins that move along cytoskeletal filaments. In particular, the microtubule-associated dynein motor is involved in the transport of organelles and vesicles, the maintenance of the Golgi, and mitosis. However, unlike kinesin and myosin, the mechanism by which dynein converts chemical energy into mechanical force remains largely a mystery, due primarily to the lack of a high-resolution molecular structure. Using homology modeling and normal mode analysis, we propose a complete atomic structure and a mechanism for force generation by the motor protein dynein. In agreement with very recent electron microscopy (EM) reconstructions showing dynein as a ring-shaped heptamer, our model consists of six ATPases of the AAA (ATPases associated with various cellular activities) superfamily and a C-terminal domain, which is experimentally known to control motor function. Our model shows a coiled coil spanning the diameter of the motor that accounts for previously unidentified structures in EM studies and provides a potential mechanism for long-range communication between the AAA domains. Furthermore, normal mode analysis reveals that the subunits of the motor that contain the nucleotide binding sites exhibit minimal movement, whereas the rest of the motor is very mobile. Our analysis suggests the likely domain rearrangements of the motor unit that generate its power stroke. This study provides insights into the structure and function of dynein that can guide further experimental investigations into energy transduction in dynein.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-10722877, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-10893253, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-11171970, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-11301258, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-11387479, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-11427534, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-11525729, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-12062019, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-12610617, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-12761065, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-12824309, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-14561776, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-15037234, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-15037250, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-15037251, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-15201901, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-15215461, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-15236967, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-15326307, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-15331592, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-15366936, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-15450294, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-15790859, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-15880123, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-16030013, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-16038997, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-16106450, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-16143512, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-16466743, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-7888180, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-9438838, http://linkedlifedata.com/resource/pubmed/commentcorrection/17121997-9927482
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
103
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18540-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
A structural model reveals energy transduction in dynein.
pubmed:affiliation
Department of Physics and Astronomy, University of North Carolina, Chapel Hill, NC 27599, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural