Solution structure of a dynein motor domain associated light chain

Abstract

Dyneins are molecular motors that translocate towards the minus ends of microtubules. In Chlamydomonas flagellar outer arm dynein, light chain 1 (LC1) associates with the nucleotide binding region within the γ heavy chain motor domain and consists of a central leucine-rich repeat section that folds as a cylindrical right handed spiral formed from six β-β-α motifs. This central cylinder is flanked by terminal helical subdomains. The C-terminal helical domain juts out from the cylinder and is adjacent to a hydrophobic surface within the repeat region that is proposed to interact with 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 spliceosome suggest that this domain interacts with the dynein motor domain.

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Figure 1: Sequence comparison and topology of LC1.
Figure 2: The NMR solution structure of LC1.
Figure 3: Electrostatic surface of LC1 and proposed heavy chain binding site.
Figure 4: LC1 interactions and architecture of the outer dynein arm.

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Acknowledgements

This study was supported by NIH grants to S.M.K. and G.P.M. and by an NIH postdoctoral fellowship to M.W.M.

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Correspondence to Gregory P. Mullen or Stephen M. King.

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Wu, H., Maciejewski, M., Marintchev, A. et al. Solution structure of a dynein motor domain associated light chain. Nat Struct Mol Biol 7, 575–579 (2000). https://doi.org/10.1038/76804

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