Solution structure of a dynein motor domain associated light chain

Dyneins are molecular motors that translocate towards the minus ends of mic rotubules. In Chlamydomonas flagellar outer arm dynein, light chain 1 (LC1) associates with the nucleotide binding region within the gamma heavy chain motor domain and consists of a central leucine-rich repeat section that fo lds as a cylindrical right handed spiral formed from six beta-beta-alpha mo tifs, This central cylinder is flanked by terminal helical subdomains. The C-terminal helical domain juts out from the cylinder and is adjacent to a h ydrophobic surface within the repeat region that is proposed to interact wi th the dynein heavy chain. The position of the C-terminal domain on LC1 and the unexpected structural similarity between LC1 and U2A' from the human s pliceosome suggest that this domain interacts with the dynein motor domain.