+検索条件
-Structure paper
タイトル | Near-atomic cryo-EM structure of PRC1 bound to the microtubule. |
---|---|
ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 113, Issue 34, Page 9430-9439, Year 2016 |
掲載日 | 2016年8月23日 |
著者 | Elizabeth H Kellogg / Stuart Howes / Shih-Chieh Ti / Erney Ramírez-Aportela / Tarun M Kapoor / Pablo Chacón / Eva Nogales / |
PubMed 要旨 | Proteins that associate with microtubules (MTs) are crucial to generate MT arrays and establish different cellular architectures. One example is PRC1 (protein regulator of cytokinesis 1), which cross- ...Proteins that associate with microtubules (MTs) are crucial to generate MT arrays and establish different cellular architectures. One example is PRC1 (protein regulator of cytokinesis 1), which cross-links antiparallel MTs and is essential for the completion of mitosis and cytokinesis. Here we describe a 4-Å-resolution cryo-EM structure of monomeric PRC1 bound to MTs. Residues in the spectrin domain of PRC1 contacting the MT are highly conserved and interact with the same pocket recognized by kinesin. We additionally found that PRC1 promotes MT assembly even in the presence of the MT stabilizer taxol. Interestingly, the angle of the spectrin domain on the MT surface corresponds to the previously observed cross-bridge angle between MTs cross-linked by full-length, dimeric PRC1. This finding, together with molecular dynamic simulations describing the intrinsic flexibility of PRC1, suggests that the MT-spectrin domain interface determines the geometry of the MT arrays cross-linked by PRC1. |
リンク | Proc Natl Acad Sci U S A / PubMed:27493215 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 3.5 Å |
構造データ | |
化合物 | ChemComp-GTP: ChemComp-MG: ChemComp-GDP: ChemComp-POU: |
由来 |
|
キーワード | STRUCTURAL PROTEIN / cytoskeleton / mitosis / microtubule / microtubule-associated protein |