3QMZ
Crystal structure of the cytoplasmic dynein heavy chain motor domain
Summary for 3QMZ
| Entry DOI | 10.2210/pdb3qmz/pdb |
| Descriptor | Cytoplasmic dynein heavy chain, Glutathione-S-transferase (2 entities in total) |
| Functional Keywords | aaa+ protein, asce protein, p-loop ntpase, cytoskeletal motor, atpase, motor protein |
| Biological source | Saccharomyces cerevisiae More |
| Cellular location | Cytoplasm, cytoskeleton: P36022 |
| Total number of polymer chains | 4 |
| Total formula weight | 622580.63 |
| Authors | Cho, C.,Carter, A.P.,Jin, L.,Vale, R.D. (deposition date: 2011-02-07, release date: 2011-03-16, Last modification date: 2026-02-11) |
| Primary citation | Carter, A.P.,Cho, C.,Jin, L.,Vale, R.D. Crystal structure of the dynein motor domain. Science, 331:1159-1165, 2011 Cited by PubMed 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. PubMed: 21330489DOI: 10.1126/science.1202393 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (6 Å) |
Structure validation
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