9J3J

Arabidopsis ATP/ADP translocator AtNTT1

9J3J の概要

• エントリーDOI: 10.2210/pdb9j3j/pdb
• EMDBエントリー: 61117
• 分子名称: ADP,ATP carrier protein 1, chloroplastic, nanobody: B-C8 (2 entities in total)
• 機能のキーワード: atp/adp translocator;non-mitochondrial;antiporter, membrane protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80355.61

構造登録者

Lin, H.J.,Huang, J.,Li, T.M.,Li, W.J.,Su, N.N.,Zhang, J.R.,Wu, X.D.,Fan, M.R. (登録日: 2024-08-08, 公開日: 2025-03-19, 最終更新日: 2025-05-21)

主引用文献

Lin, H.,Huang, J.,Li, T.,Li, W.,Wu, Y.,Yang, T.,Nian, Y.,Lin, X.,Wang, J.,Wang, R.,Zhao, X.,Su, N.,Zhang, J.,Wu, X.,Fan, M.
Structure and mechanism of the plastid/parasite ATP/ADP translocator.
Nature, 641:797-804, 2025

PubMed Abstract: Adenosine triphosphate (ATP) is the principal energy currency of all living cells. Metabolically impaired obligate intracellular parasites, such as the human pathogens Chlamydia trachomatis and Rickettsia prowazekii, can acquire ATP from their host cells through a unique ATP/adenosine diphosphate (ADP) translocator, which mediates the import of ATP into and the export of ADP and phosphate out of the parasite cells, thus allowing the exploitation of the energy reserves of host cells (also known as energy parasitism). This type of ATP/ADP translocator also exists in the obligate intracellular endosymbionts of protists and the plastids of plants and algae and has been implicated to play an important role in endosymbiosis. The plastid/parasite type of ATP/ADP translocator is phylogenetically and functionally distinct from the mitochondrial ATP/ADP translocator, and its structure and transport mechanism are still unknown. Here we report the cryo-electron microscopy structures of two plastid/parasite types of ATP/ADP translocators in the apo and substrate-bound states. The ATP/ADP-binding pocket is located at the interface between the N and C domains of the translocator, and a conserved asparagine residue within the pocket is critical for substrate specificity. The translocator operates through a rocker-switch alternating access mechanism involving the relative rotation of the two domains as rigid bodies. Our results provide critical insights for understanding ATP translocation across membranes in energy parasitism and endosymbiosis and offer a structural basis for developing drugs against obligate intracellular parasites.

PubMed: 40074904
DOI: 10.1038/s41586-025-08743-3

実験手法

ELECTRON MICROSCOPY (2.83 Å)