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Structure paper

TitleStructure and functional role of dynein's microtubule-binding domain.
Journal, issue, pagesScience, Vol. 322, Issue 5908, Page 1691-1695, Year 2008
Publish dateDec 12, 2008
AuthorsAndrew P Carter / Joan E Garbarino / Elizabeth M Wilson-Kubalek / Wesley E Shipley / Carol Cho / Ronald A Milligan / Ronald D Vale / I R Gibbons /
PubMed AbstractDynein motors move various cargos along microtubules within the cytoplasm and power the beating of cilia and flagella. An unusual feature of dynein is that its microtubule-binding domain (MTBD) is ...Dynein motors move various cargos along microtubules within the cytoplasm and power the beating of cilia and flagella. An unusual feature of dynein is that its microtubule-binding domain (MTBD) is separated from its ring-shaped AAA+ adenosine triphosphatase (ATPase) domain by a 15-nanometer coiled-coil stalk. We report the crystal structure of the mouse cytoplasmic dynein MTBD and a portion of the coiled coil, which supports a mechanism by which the ATPase domain and MTBD may communicate through a shift in the heptad registry of the coiled coil. Surprisingly, functional data suggest that the MTBD, and not the ATPase domain, is the main determinant of the direction of dynein motility.
External linksScience / PubMed:19074350 / PubMed Central
MethodsEM (helical sym.) / X-ray diffraction
Resolution2.27 - 35.0 Å
Structure data

EMDB-1581:
Structure and functional role of dynein's microtubule-binding domain
Method: EM (helical sym.) / Resolution: 35.0 Å

PDB-3err:
Microtubule binding domain from mouse cytoplasmic dynein as a fusion with seryl-tRNA synthetase
Method: X-RAY DIFFRACTION / Resolution: 2.27 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM / Adenosine monophosphate

ChemComp-HOH:
WATER / Water

Source
  • mus musculus (house mouse)
  • thermus thermophilus (bacteria)
KeywordsLIGASE / dynein / microtubule binding domain / coiled coil / fusion protein

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