5FCM

CrBld10-N 1-70

5FCM の概要

• エントリーDOI: 10.2210/pdb5fcm/pdb
• 分子名称: Basal body protein, ISOPROPYL ALCOHOL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: centriole, centrosome, cep135, bld10, cartwheel, cell cycle
• 由来する生物種: Chlamydomonas reinhardtii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 32340.74

構造登録者

Kraatz, S.H.W.,Steinmetz, M.O. (登録日: 2015-12-15, 公開日: 2016-07-20, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.229 Å)