8HBR
The C-terminal domain of Spiral2
8HBR の概要
エントリーDOI | 10.2210/pdb8hbr/pdb |
分子名称 | TOG domain-containing protein (2 entities in total) |
機能のキーワード | microtubule associated protein, structural protein |
由来する生物種 | Physcomitrium patens |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 91220.31 |
構造登録者 | |
主引用文献 | Ohno, M.,Higuchi, Y.,Hayashi, I. Crystal structure of the C-terminal domain of the plant-specific microtubule-associated protein Spiral2. Acta Crystallogr.,Sect.F, 79:17-22, 2023 Cited by PubMed Abstract: Plant cells form microtubule arrays, called `cortical microtubules', beneath the plasma membrane which are critical for cell-wall organization and directional cell growth. Cortical microtubules are nucleated independently of centrosomes. Spiral2 is a land-plant-specific microtubule minus-end-targeting protein that stabilizes the minus ends by inhibiting depolymerization of the filament. Spiral2 possesses an N-terminal microtubule-binding domain and a conserved C-terminal domain whose function is unknown. In this study, the crystal structure of the conserved C-terminal domain of Spiral2 was determined using the single-wavelength anomalous dispersion method. Refinement of the model to a resolution of 2.2 Å revealed a helix-turn-helix fold with seven α-helices. The protein crystallized as a dimer, but SEC-MALS analysis showed the protein to be monomeric. A structural homology search revealed that the protein has similarity to the C-terminal domain of the katanin regulatory subunit p80. The structure presented here suggests that the C-terminal domain of Spiral2 represents a new class of microtubule dynamics modulator across the kingdom. PubMed: 36598352DOI: 10.1107/S2053230X22011815 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード