Structure and mechanism of the plastid/parasite ATP/ADP translocator

Huajian Lin, Jian Huang, Tianming Li, Wenjuan Li, Yutong Wu, Tianjiao Yang, Yuwei Nian, Xiang Lin, Jiangqin Wang, Ruiying Wang, Xiaohui Zhao, Nannan Su (), Jinru Zhang (), Xudong Wu () and Minrui Fan ()
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Huajian Lin: Chinese Academy of Sciences
Jian Huang: Westlake University
Tianming Li: Chinese Academy of Sciences
Wenjuan Li: Chinese Academy of Sciences
Yutong Wu: Chinese Academy of Sciences
Tianjiao Yang: Chinese Academy of Sciences
Yuwei Nian: Chinese Academy of Sciences
Xiang Lin: Fudan University
Jiangqin Wang: Zhejiang University
Ruiying Wang: Chinese Academy of Sciences
Xiaohui Zhao: Chinese Academy of Sciences
Nannan Su: Zhejiang University
Jinru Zhang: Fudan University
Xudong Wu: Westlake University
Minrui Fan: Chinese Academy of Sciences

Nature, 2025, vol. 641, issue 8063, 797-804

Abstract: Abstract Adenosine triphosphate (ATP) is the principal energy currency of all living cells1,2. 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 endosymbiosis3–31. 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.

Date: 2025
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DOI: 10.1038/s41586-025-08743-3

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