1DS9
SOLUTION STRUCTURE OF CHLAMYDOMONAS OUTER ARM DYNEIN LIGHT CHAIN 1
1DS9 の概要
エントリーDOI | 10.2210/pdb1ds9/pdb |
NMR情報 | BMRB: 4265 |
分子名称 | OUTER ARM DYNEIN (1 entity in total) |
機能のキーワード | leucine-rich repeat, beta-beta-alpha cylinder, dynein, chlamydomonas, flagella, contractile protein |
由来する生物種 | Chlamydomonas reinhardtii |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 22179.57 |
構造登録者 | Wu, H.W.,Maciejewski, M.W.,Marintchev, A.,Benashski, S.E.,Mullen, G.P.,King, S.M. (登録日: 2000-01-07, 公開日: 2000-07-26, 最終更新日: 2024-05-22) |
主引用文献 | 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 Cited by 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: 10876244DOI: 10.1038/76804 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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