6BL7

S. cerevisiae stu2 coiled coil domain

6BL7 の概要

• エントリーDOI: 10.2210/pdb6bl7/pdb
• 分子名称: Protein STU2 (2 entities in total)
• 機能のキーワード: kinetochore microtubule polymerase microtubule associated protein coiled coil, structural protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27579.49

構造登録者

Slep, K.C. (登録日: 2017-11-09, 公開日: 2017-12-13, 最終更新日: 2024-10-16)

主引用文献

Haase, K.P.,Fox, J.C.,Byrnes, A.E.,Adikes, R.C.,Speed, S.K.,Haase, J.,Friedman, B.,Cook, D.M.,Bloom, K.,Rusan, N.M.,Slep, K.C.
Stu2 uses a 15-nm parallel coiled coil for kinetochore localization and concomitant regulation of the mitotic spindle.
Mol. Biol. Cell, 29:285-294, 2018

PubMed Abstract: XMAP215/Dis1 family proteins are potent microtubule polymerases, critical for mitotic spindle structure and dynamics. While microtubule polymerase activity is driven by an N-terminal tumor overexpressed gene (TOG) domain array, proper cellular localization is a requisite for full activity and is mediated by a C-terminal domain. Structural insight into the C-terminal domain's architecture and localization mechanism remain outstanding. We present the crystal structure of the Stu2 C-terminal domain, revealing a 15-nm parallel homodimeric coiled coil. The parallel architecture of the coiled coil has mechanistic implications for the arrangement of the homodimer's N-terminal TOG domains during microtubule polymerization. The coiled coil has two spatially distinct conserved regions: CRI and CRII. Mutations in CRI and CRII perturb the distribution and localization of Stu2 along the mitotic spindle and yield defects in spindle morphology including increased frequencies of mispositioned and fragmented spindles. Collectively, these data highlight roles for the Stu2 dimerization domain as a scaffold for factor binding that optimally positions Stu2 on the mitotic spindle to promote proper spindle structure and dynamics.

PubMed: 29187574
DOI: 10.1091/mbc.E17-01-0057

実験手法

X-RAY DIFFRACTION (2.5 Å)