4W7G

Crystal Structure of the Dynein Light Intermediate Chain's Conserved Domain

Summary for 4W7G

• Entry DOI: 10.2210/pdb4w7g/pdb
• Descriptor: Dynein Light Intermediate Chain (2 entities in total)
• Functional Keywords: molecular motor, g protein, intracellular motility, dynein subunit, motor protein
• Biological source: Chaetomium thermophilum
• Total number of polymer chains: 1
• Total formula weight: 61130.39

Authors

Schroeder, C.M.,Ekiert, D.C.,Vale, R.D. (deposition date: 2014-08-22, release date: 2014-10-01, Last modification date: 2023-12-27)

Primary citation

Schroeder, C.M.,Ostrem, J.M.,Hertz, N.T.,Vale, R.D.
A Ras-like domain in the light intermediate chain bridges the dynein motor to a cargo-binding region.
Elife, 3:e03351-e03351, 2014

PubMed Abstract: Cytoplasmic dynein, a microtubule-based motor protein, transports many intracellular cargos by means of its light intermediate chain (LIC). In this study, we have determined the crystal structure of the conserved LIC domain, which binds the motor heavy chain, from a thermophilic fungus. We show that the LIC has a Ras-like fold with insertions that distinguish it from Ras and other previously described G proteins. Despite having a G protein fold, the fungal LIC has lost its ability to bind nucleotide, while the human LIC1 binds GDP preferentially over GTP. We show that the LIC G domain binds the dynein heavy chain using a conserved patch of aromatic residues, whereas the less conserved C-terminal domain binds several Rab effectors involved in membrane transport. These studies provide the first structural information and insight into the evolutionary origin of the LIC as well as revealing how this critical subunit connects the dynein motor to cargo.

PubMed: 25272277
DOI: 10.7554/eLife.03351

Experimental method

X-RAY DIFFRACTION (2.1 Å)