5FCM

CrBld10-N 1-70

Summary for 5FCM

• Entry DOI: 10.2210/pdb5fcm/pdb
• Descriptor: Basal body protein, ISOPROPYL ALCOHOL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: centriole, centrosome, cep135, bld10, cartwheel, cell cycle
• Biological source: Chlamydomonas reinhardtii
• Total number of polymer chains: 4
• Total formula weight: 32340.74

Authors

Kraatz, S.H.W.,Steinmetz, M.O. (deposition date: 2015-12-15, release date: 2016-07-20, Last modification date: 2024-05-08)

Primary citation

Kraatz, S.,Guichard, P.,Obbineni, J.M.,Olieric, N.,Hatzopoulos, G.N.,Hilbert, M.,Sen, I.,Missimer, J.,Gonczy, P.,Steinmetz, M.O.
The Human Centriolar Protein CEP135 Contains a Two-Stranded Coiled-Coil Domain Critical for Microtubule Binding.
Structure, 24:1358-1371, 2016

PubMed Abstract: Centrioles are microtubule-based structures that play important roles notably in cell division and cilium biogenesis. CEP135/Bld10p family members are evolutionarily conserved microtubule-binding proteins important for centriole formation. Here, we analyzed in detail the microtubule-binding activity of human CEP135 (HsCEP135). X-ray crystallography and small-angle X-ray scattering in combination with molecular modeling revealed that the 158 N-terminal residues of HsCEP135 (HsCEP135-N) form a parallel two-stranded coiled-coil structure. Biochemical, cryo-electron, and fluorescence microscopy analyses revealed that in vitro HsCEP135-N interacts with tubulin, protofilaments, and microtubules and induces the formation of microtubule bundles. We further identified a 13 amino acid segment spanning residues 96-108, which represents a major microtubule-binding site in HsCEP135-N. Within this segment, we identified a cluster of three lysine residues that contribute to the microtubule bundling activity of HsCEP135-N. Our results provide the first structural information on CEP135/Bld10p proteins and offer insights into their microtubule-binding mechanism.

PubMed: 27477386
DOI: 10.1016/j.str.2016.06.011

Experimental method

X-RAY DIFFRACTION (2.229 Å)