3QMZ: Crystal Structure of the Cytoplasmic Dynein Heavy Chain Motor Domain

Citation:
Abstract
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 ~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.
PDB ID: 3QMZDownload
MMDB ID: 89272
PDB Deposition Date: 2011/2/7
Updated in MMDB: 2011/06 
Experimental Method:
x-ray diffraction
Resolution: 6  Å
Source Organism:
Schistosoma japonicum
Similar Structures:
Biological Unit for 3QMZ: dimeric; determined by author
Molecular Components in 3QMZ
Label Count Molecule
Proteins (2 molecules)
1
Cytoplasmic Dynein Heavy Chain
(Gene: DYN1)
Molecule annotation
1
Glutathione-s-transferase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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