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Literature summary for 5.6.1.2 extracted from
- Crystal structure of the dynein motor domain (2011), Science, 331, 1159-1165.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant protein | Saccharomyces cerevisiae |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| resolution of 6 A of a functional dimer of two ca. 300 kDa motor domains of yeast cytoplasmic dynein, which are dimerized by glutathione S-transferase GST. The structure reveals an unusual asymmetric arrangement of ATPase domains and an unexpected interaction between two coiled coils the create a base for the microtubule binding domain | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dynein | - |
Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | dyneins are microtubule-based motor proteins that power ciliary beating, transport intracellular cargos, and help to construct the mitotic spindle | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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