3MXZ

Crystal Structure of tubulin folding cofactor A from Arabidopsis thaliana

3MXZ の概要

• エントリーDOI: 10.2210/pdb3mxz/pdb
• 分子名称: Tubulin-specific chaperone A, NITRATE ION (3 entities in total)
• 機能のキーワード: helix bundle, chaperone
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13252.80

構造登録者

Lu, L.,Nan, J.,Mi, W.,Su, X.D.,Li, Y. (登録日: 2010-05-08, 公開日: 2010-09-01, 最終更新日: 2023-11-01)

主引用文献

Lu, L.,Nan, J.,Mi, W.,Li, L.F.,Wei, C.H.,Su, X.D.,Li, Y.
Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its beta-tubulin binding characterization
Febs Lett., 584:3533-3539, 2010

PubMed Abstract: Microtubules are composed of polymerized alpha/beta-tubulin heterodimers. Biogenesis of assembly-competent tubulin dimers is a complex multistep process that requires sequential actions of distinct molecular chaperones and cofactors. Tubulin folding cofactor A (TFCA), which captures beta-tubulin during the folding pathway, has been identified in many organisms. Here, we report the crystal structure of Arabidopsis thaliana TFC A (KIESEL, KIS), which forms a monomeric three-helix bundle. The functional binding analysis demonstrated that KIS interacts with beta-tubulin in plant. Furthermore, mutagenesis studies indicated that the alpha-helical regions of KIS participate in beta-tubulin binding. Unlike the budding yeast TFC A, the two loop regions of KIS are not required for this interaction suggesting a distinct binding mechanism of TFC A to beta-tubulin in plants.

PubMed: 20638386
DOI: 10.1016/j.febslet.2010.07.017

実験手法

X-RAY DIFFRACTION (1.599 Å)