Crystal Structure of the Dynein Motor Domain

Cited 148 time in webofscience Cited 0 time in scopus
  • Hit : 59
  • Download : 0
Dyneins are microtubule-based motor proteins that power ciliary beating, transport intracellular cargos, and help to construct the mitotic spindle. Evolved from ring-shaped hexameric AAA-family adenosine triphosphatases (ATPases), dynein's large size and complexity have posed challenges for understanding its structure and mechanism. Here, we present a 6 angstrom crystal structure of a functional dimer of two similar to 300-kilodalton motor domains of yeast cytoplasmic dynein. The structure reveals an unusual asymmetric arrangement of ATPase domains in the ring-shaped motor domain, the manner in which the mechanical element interacts with the ATPase ring, and an unexpected interaction between two coiled coils that create a base for the microtubule binding domain. The arrangement of these elements provides clues as to how adenosine triphosphate-driven conformational changes might be transmitted across the motor domain.
Publisher
AMER ASSOC ADVANCEMENT SCIENCE
Issue Date
2011-03
Language
English
Article Type
Article
Keywords

MICROTUBULE-BINDING DOMAIN; REPLICATIVE HEXAMERIC HELICASE; CYTOPLASMIC DYNEIN; SACCHAROMYCES-CEREVISIAE; CONFORMATIONAL-CHANGE; ENERGY TRANSDUCTION; COILED-COIL; MECHANISMS; PROTEINS; MOTIONS

Citation

SCIENCE, v.331, no.6021, pp.1159 - 1165

ISSN
0036-8075
DOI
10.1126/science.1202393
URI
http://hdl.handle.net/10203/207334
Appears in Collection
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 148 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0