2OF3

TOG domain structure from C.elegans Zyg9

2OF3 の概要

• エントリーDOI: 10.2210/pdb2of3/pdb
• 分子名称: ZYG-9 (2 entities in total)
• 機能のキーワード: multifunctional macromolecule, kinetochore, microtubule, xmap215, zyg9, stu2, dis1, microtubule associated protein, structural protein, cell cycle
• 由来する生物種: Caenorhabditis elegans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30013.93

構造登録者

Al-Bassam, J.,Larsen, N.A.,Hyman, A.A.,Harrison, S.C. (登録日: 2007-01-02, 公開日: 2007-03-13, 最終更新日: 2023-12-27)

主引用文献

Al-Bassam, J.,Larsen, N.A.,Hyman, A.A.,Harrison, S.C.
Crystal structure of a TOG domain: conserved features of XMAP215/Dis1-family TOG domains and implications for tubulin binding.
Structure, 15:355-362, 2007

PubMed Abstract: Members of the XMAP215/Dis1 family of microtubule-associated proteins (MAPs) are essential for microtubule growth. MAPs in this family contain several 250 residue repeats, called TOG domains, which are thought to bind tubulin dimers and promote microtubule polymerization. We have determined the crystal structure of a single TOG domain from the Caenorhabditis elegans homolog, Zyg9, to 1.9 A resolution, and from it we describe a structural blueprint for TOG domains. These domains are flat, paddle-like structures, composed of six HEAT-repeat elements stacked side by side. The two wide faces of the paddle contain the HEAT-repeat helices, and the two narrow faces, the intra- and inter-HEAT repeat turns. Solvent-exposed residues in the intrarepeat turns are conserved, both within a particular protein and across the XMAP215/Dis1 family. Mutation of some of these residues in the TOG1 domain from the budding yeast homolog, Stu2p, shows that this face indeed participates in the tubulin contact.

PubMed: 17355870
DOI: 10.1016/j.str.2007.01.012

実験手法

X-RAY DIFFRACTION (1.9 Å)