5KMG

Near-atomic cryo-EM structure of PRC1 bound to the microtubule

5KMG の概要

• エントリーDOI: 10.2210/pdb5kmg/pdb
• 関連するPDBエントリー: 2NRY 3NRX
• EMDBエントリー: 8266
• 分子名称: Tubulin alpha-1B chain, Tubulin beta chain, Protein regulator of cytokinesis 1, ... (7 entities in total)
• 機能のキーワード: cytoskeleton, mitosis, microtubule, microtubule-associated protein, structural protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 114628.02

構造登録者

Kellogg, E.H.,Howes, S.,Ti, S.-C.,Ramirez-Aportela, E.,Kapoor, T.M.,Chacon, P.,Nogales, E. (登録日: 2016-06-27, 公開日: 2016-08-03, 最終更新日: 2024-03-06)

主引用文献

Kellogg, E.H.,Howes, S.,Ti, S.C.,Ramirez-Aportela, E.,Kapoor, T.M.,Chacon, P.,Nogales, E.
Near-atomic cryo-EM structure of PRC1 bound to the microtubule.
Proc.Natl.Acad.Sci.USA, 113:9430-9439, 2016

PubMed Abstract: 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.

PubMed: 27493215
DOI: 10.1073/pnas.1609903113

実験手法

ELECTRON MICROSCOPY (3.5 Å)