Solution structure of a dynein motor domain associated light chain

Nat Struct Biol. 2000 Jul;7(7):575-9. doi: 10.1038/76804.

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.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Chlamydomonas reinhardtii / chemistry*
  • Chlamydomonas reinhardtii / cytology
  • Dyneins / chemistry*
  • Dyneins / metabolism*
  • Flagella / chemistry
  • Humans
  • Microtubule-Associated Proteins / chemistry
  • Microtubule-Associated Proteins / metabolism
  • Models, Molecular
  • Molecular Motor Proteins / chemistry*
  • Molecular Motor Proteins / metabolism*
  • Molecular Sequence Data
  • Molecular Weight
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Binding
  • Protein Structure, Secondary
  • Ribonucleoprotein, U2 Small Nuclear / chemistry
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Solutions
  • Structure-Activity Relationship
  • Surface Properties

Substances

  • Microtubule-Associated Proteins
  • Molecular Motor Proteins
  • Ribonucleoprotein, U2 Small Nuclear
  • Solutions
  • U2A' protein, human
  • Dyneins

Associated data

  • PDB/1DS9