PDBsum entry 4lzf

Structural protein, protein binding

PDB id: 4lzf

Contents

Protein chains

155 a.a.

12 a.a.

Ligands

PGE

MPD ×2

PG4

Waters ×99

PDB id:

4lzf

Name:

Structural protein, protein binding

Title:

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

Structure:

Centrosomal p4.1-associated protein. Chain: a. Fragment: unp residues 942-1121. Engineered: yes. Scl-interrupting locus protein homolog. Chain: b. Fragment: unp residues 414-428. Engineered: yes

Source:

Danio rerio. Leopard danio,zebra danio,zebra fish. Organism_taxid: 7955. Gene: cenpj. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Organism_taxid: 7955

Resolution:

1.72Å R-factor: 0.192 R-free: 0.231

Authors:

G.N.Hatzopoulos,M.C.Erat,E.Cutts,K.Rogala,L.Slatter,P.J.Stansfeld, I.Vakonakis

Key ref:

G.N.Hatzopoulos et al. (2013). Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structure, 21, 2069-2077. PubMed id: 24076405 DOI: 10.1016/j.str.2013.08.019

Date:

31-Jul-13 Release date: 11-Sep-13

Protein chain

E7FCY1  (E7FCY1_DANRE) -  Centromere protein J from Danio rerio

Seq: 1124 a.a.

Struc: 155 a.a.

Protein chain

Q8JGS1  (STIL_DANRE) -  SCL-interrupting locus protein homolog from Danio rerio

Seq: 1263 a.a.

Struc: 12 a.a.

DOI no: 10.1016/j.str.2013.08.019

Structure 21:2069-2077 (2013)

PubMed id: 24076405

Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture.

G.N.Hatzopoulos, M.C.Erat, E.Cutts, K.B.Rogala, L.M.Slater, P.J.Stansfeld, I.Vakonakis.

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.