6L5J

Crystal structure of human rootletin 1108-1317

Summary for 6L5J

• Entry DOI: 10.2210/pdb6l5j/pdb
• Descriptor: Rootletin (1 entity in total)
• Functional Keywords: centrosome, rootletin, coiled-coil, structural protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 4
• Total formula weight: 100473.76

Authors

Kim, J.,Choi, H.J. (deposition date: 2019-10-23, release date: 2020-07-29)

Primary citation

Ko, D.,Kim, J.,Rhee, K.,Choi, H.J.
Identification of a Structurally Dynamic Domain for Oligomer Formation in Rootletin.
J.Mol.Biol., 432:3915-3932, 2020

PubMed Abstract: Rootletin is the main component of the ciliary rootlet and functions as a centriole linker connecting the two mother centrioles. Despite the functional importance of rootletin, the molecular architecture of the rootletin filament and its assembly mechanism are poorly understood. Here, we identify the coiled-coil domain 3 (CCD3) of rootletin as the key domain for its cellular function. The crystal structure of the CCD3 fragment containing 28 heptad repeats and 1 hendecad repeat reveals that it forms a parallel coiled-coil dimer spanning approximately 300 Å in length. Crosslinking experiments and biophysical analyses of the minimal functional region of CCD3 (CCD3-6) suggest that CCD3-6 is structurally dynamic and may be important for oligomer formation. We also show that oligomerization-defective CCD3 mutants fail in centrosomal localization and centriole linkage, suggesting that rootletin oligomerization may be important for its function.

PubMed: 32325071
DOI: 10.1016/j.jmb.2020.04.012

Experimental method

X-RAY DIFFRACTION (2.77 Å)