6HXT

Crystal structure of the head domain of human CCDC61

Summary for 6HXT

• Entry DOI: 10.2210/pdb6hxt/pdb
• Descriptor: Coiled-coil domain-containing protein 61 (2 entities in total)
• Functional Keywords: centrosome, cilia, scaffold protein, protfilament, structural protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 3
• Total formula weight: 50211.49

Authors

Ochi, T.,Blundell, T.L.,van Breugel, M. (deposition date: 2018-10-18, release date: 2020-04-29, Last modification date: 2024-10-23)

Primary citation

Ochi, T.,Quarantotti, V.,Lin, H.,Jullien, J.,Rosa E Silva, I.,Boselli, F.,Barnabas, D.D.,Johnson, C.M.,McLaughlin, S.H.,Freund, S.M.V.,Blackford, A.N.,Kimata, Y.,Goldstein, R.E.,Jackson, S.P.,Blundell, T.L.,Dutcher, S.K.,Gergely, F.,van Breugel, M.
CCDC61/VFL3 Is a Paralog of SAS6 and Promotes Ciliary Functions.
Structure, 28:674-, 2020

PubMed Abstract: Centrioles are cylindrical assemblies whose peripheral microtubule array displays a 9-fold rotational symmetry that is established by the scaffolding protein SAS6. Centriole symmetry can be broken by centriole-associated structures, such as the striated fibers in Chlamydomonas that are important for ciliary function. The conserved protein CCDC61/VFL3 is involved in this process, but its exact role is unclear. Here, we show that CCDC61 is a paralog of SAS6. Crystal structures of CCDC61 demonstrate that it contains two homodimerization interfaces that are similar to those found in SAS6, but result in the formation of linear filaments rather than rings. Furthermore, we show that CCDC61 binds microtubules and that residues involved in CCDC61 microtubule binding are important for ciliary function in Chlamydomonas. Together, our findings suggest that CCDC61 and SAS6 functionally diverged from a common ancestor while retaining the ability to scaffold the assembly of basal body-associated structures or centrioles, respectively.

PubMed: 32375023
DOI: 10.1016/j.str.2020.04.010

Experimental method

X-RAY DIFFRACTION (2.55 Å)