5X2D

Crystal structure of DLC like domain of CsTAL3 (83-177aa)

5X2D の概要

• エントリーDOI: 10.2210/pdb5x2d/pdb
• 関連するPDBエントリー: 5X2E
• 分子名称: Tegumental protein 20.8 kDa (2 entities in total)
• 機能のキーワード: calcium-binding protein, tegument protein, cstal3, dynein light chain, cell adhesion
• 由来する生物種: Clonorchis sinensis (Chinese liver fluke)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 32400.61

構造登録者

Jo, C.H.,Hwang, K.Y. (登録日: 2017-01-31, 公開日: 2017-08-30, 最終更新日: 2024-04-03)

主引用文献

Jo, C.H.,Son, J.,Kim, S.,Oda, T.,Kim, J.,Lee, M.R.,Sato, M.,Kim, H.T.,Unzai, S.,Park, S.Y.,Hwang, K.Y.
Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis
Sci Rep, 7:1764-1764, 2017

PubMed Abstract: Survival of Clonorchis sinensis, a cause of human clonorchiasis, requires tegument proteins, which are localized to the tegumental outer surface membrane. These proteins play an important role in a host response and parasite survival. Thus, these proteins are interesting molecular targets for vaccine and drug development. Here, we have determined two crystal structures of the calmodulin like domain (amino acid [aa] positions 1-81) and dynein light chain (DLC)-like domain (aa 83-177) of a 20.8-kDa tegumental-allergen-like protein from Clonorchis sinensis (CsTAL3). The calmodulin like domain has two Ca-binding sites (named CB1 and CB2), but Ca binds to only one site, CB1. The DLC-like domain has a dimeric conformation; the interface is formed mainly by hydrogen bonds between the main chain atoms. In addition, we have determined full-length structure of CsTAL3 in solution and showed the conformational change of CsTAL3 induced by Ca ion binding using small-angle X-ray scattering analysis and molecular dynamics simulations. The Ca-bound form has a more extended conformation than the Ca-free from does. These structural and biochemical analyses will advance the understanding of the biology of this liver fluke and may contribute to our understanding of the molecular mechanism of calcium-responsive and tegumental-allergen-like proteins.

PubMed: 28496122
DOI: 10.1038/s41598-017-02044-0

実験手法

X-RAY DIFFRACTION (2.6 Å)