1DS9

SOLUTION STRUCTURE OF CHLAMYDOMONAS OUTER ARM DYNEIN LIGHT CHAIN 1

Summary for 1DS9

• Entry DOI: 10.2210/pdb1ds9/pdb
• NMR Information: BMRB: 4265
• Descriptor: OUTER ARM DYNEIN (1 entity in total)
• Functional Keywords: leucine-rich repeat, beta-beta-alpha cylinder, dynein, chlamydomonas, flagella, contractile protein
• Biological source: Chlamydomonas reinhardtii
• Total number of polymer chains: 1
• Total formula weight: 22179.57

Authors

Wu, H.W.,Maciejewski, M.W.,Marintchev, A.,Benashski, S.E.,Mullen, G.P.,King, S.M. (deposition date: 2000-01-07, release date: 2000-07-26, Last modification date: 2024-05-22)

Primary citation

Wu, H.,Maciejewski, M.W.,Marintchev, A.,Benashski, S.E.,Mullen, G.P.,King, S.M.
Solution structure of a dynein motor domain associated light chain.
Nat.Struct.Biol., 7:575-579, 2000

PubMed 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 gamma heavy chain motor domain and consists of a central leucine-rich repeat section that folds as a cylindrical right handed spiral formed from six beta-beta-alpha 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.

PubMed: 10876244
DOI: 10.1038/76804

Experimental method

SOLUTION NMR