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Centrioles are evolutionarily conserved eukaryotic organelles composed of a protein scaffold surrounded by sets of microtubules organized with a 9-fold radial symmetry. CPAP, a centriolar protein essential for microtubule recruitment, features a C-terminal domain of unknown structure, the G-box. A missense mutation in the G-box reduces affinity for the centriolar shuttling protein STIL and causes primary microcephaly. Here, we characterize the molecular architecture of CPAP and determine the G-box structure alone and in complex with a STIL fragment. The G-box comprises a single elongated β sheet capable of forming supramolecular assemblies. Structural and biophysical studies highlight the conserved nature of the CPAP-STIL complex. We propose that CPAP acts as a horizontal "strut" that joins the centriolar scaffold with microtubules, whereas G-box domains form perpendicular connections.

Original publication

DOI

10.1016/j.str.2013.08.019

Type

Journal article

Journal

Structure

Publication Date

05/11/2013

Volume

21

Pages

2069 - 2077

Keywords

Animals, Centrioles, Crystallography, X-Ray, Humans, Microcephaly, Microtubule-Associated Proteins, Models, Molecular, Mutation, Missense, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Zebrafish, Zebrafish Proteins