4LZF

A novel domain in the microcephaly protein CPAP suggests a role in centriole architecture

Summary for 4LZF

• Entry DOI: 10.2210/pdb4lzf/pdb
• Related: 4LD1 4LD3
• Descriptor: Centrosomal P4.1-associated protein, SCL-interrupting locus protein homolog, TRIETHYLENE GLYCOL, ... (6 entities in total)
• Functional Keywords: g-box, beta-sheet, centriole organisation, structural protein, protein binding
• Biological source: Danio rerio (leopard danio,zebra danio,zebra fish); More
• Cellular location: Cytoplasm : Q8JGS1
• Total number of polymer chains: 2
• Total formula weight: 23070.85

Authors

Hatzopoulos, G.N.,Erat, M.C.,Cutts, E.,Rogala, K.,Slatter, L.,Stansfeld, P.J.,Vakonakis, I. (deposition date: 2013-07-31, release date: 2013-09-11, Last modification date: 2023-09-20)

Primary citation

Hatzopoulos, G.N.,Erat, M.C.,Cutts, E.,Rogala, K.B.,Slater, L.M.,Stansfeld, P.J.,Vakonakis, I.
Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture.
Structure, 21:2069-2077, 2013

PubMed Abstract: 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.

PubMed: 24076405
DOI: 10.1016/j.str.2013.08.019

Experimental method

X-RAY DIFFRACTION (1.72 Å)