3OA7

Structure of the C-terminal domain of Cnm67, a core component of the spindle pole body of Saccharomyces cerevisiae

3OA7 の概要

• エントリーDOI: 10.2210/pdb3oa7/pdb
• 分子名称: Head morphogenesis protein, Chaotic nuclear migration protein 67 fusion protein (2 entities in total)
• 機能のキーワード: coiled coils, structural protein, spindle pole body
• 由来する生物種: Bacillus phage phi29 (virus, yeast); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body : P53865
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24281.71

構造登録者

Klenchin, V.A.,Frye, J.J.,Rayment, I. (登録日: 2010-08-04, 公開日: 2011-03-23, 最終更新日: 2024-10-30)

主引用文献

Klenchin, V.A.,Frye, J.J.,Jones, M.H.,Winey, M.,Rayment, I.
Structure-function analysis of the C-terminal domain of CNM67, a core component of the Saccharomyces cerevisiae spindle pole body.
J.Biol.Chem., 286:18240-18250, 2011

PubMed Abstract: The spindle pole body of the budding yeast Saccharomyces cerevisiae has served as a model system for understanding microtubule organizing centers, yet very little is known about the molecular structure of its components. We report here the structure of the C-terminal domain of the core component Cnm67 at 2.3 Å resolution. The structure determination was aided by a novel approach to crystallization of proteins containing coiled-coils that utilizes globular domains to stabilize the coiled-coils. This enhances their solubility in Escherichia coli and improves their crystallization. The Cnm67 C-terminal domain (residues Asn-429-Lys-581) exhibits a previously unseen dimeric, interdigitated, all α-helical fold. In vivo studies demonstrate that this domain alone is able to localize to the spindle pole body. In addition, the structure reveals a large functionally indispensable positively charged surface patch that is implicated in spindle pole body localization. Finally, the C-terminal eight residues are disordered but are critical for protein folding and structural stability.

PubMed: 21454609
DOI: 10.1074/jbc.M111.227371

実験手法

X-RAY DIFFRACTION (2.3 Å)