6FND
Crystal structure of Toxoplasma gondii AKMT
6FND の概要
| エントリーDOI | 10.2210/pdb6fnd/pdb |
| 分子名称 | Apical complex lysine methyltransferase, ZINC ION, SULFATE ION, ... (10 entities in total) |
| 機能のキーワード | lysine methyltransferase, set domain, akmt, homodimer, transferase |
| 由来する生物種 | Toxoplasma gondii 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 196262.02 |
| 構造登録者 | |
| 主引用文献 | Pivovarova, Y.,Liu, J.,Lesigang, J.,Koldyka, O.,Rauschmeier, R.,Hu, K.,Dong, G. Structure of a Novel Dimeric SET Domain Methyltransferase that Regulates Cell Motility. J. Mol. Biol., 430:4209-4229, 2018 Cited by PubMed Abstract: Lysine methyltransferases (KMTs) were initially associated with transcriptional control through their methylation of histones and other nuclear proteins, but have since been found to regulate many other cellular activities. The apical complex lysine (K) methyltransferase (AKMT) of the human parasite Toxoplasma gondii was recently shown to play a critical role in regulating cellular motility. Here we report a 2.1-Å resolution crystal structure of the conserved and functional C-terminal portion (aa289-709) of T. gondii AKMT. AKMT dimerizes via a unique intermolecular interface mediated by the C-terminal tetratricopeptide repeat-like domain together with a specific zinc-binding motif that is absent from all other KMTs. Disruption of AKMT dimerization impaired both its enzyme activity and parasite egress from infected host cells in vivo. Structural comparisons reveal that AKMT is related to the KMTs in the SMYD family, with, however, a number of distinct structural features in addition to the unusual dimerization interface. These features are conserved among the apicomplexan parasites and their free-living relatives, but not found in any known KMTs in animals. AKMT therefore is the founding member of a new subclass of KMT that has important implications for the evolution of the apicomplexans. PubMed: 30148980DOI: 10.1016/j.jmb.2018.08.017 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.101 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






