Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure and mechanism of the plastid/parasite ATP/ADP translocator.
Journal, issue, pages	Nature, Vol. 641, Issue 8063, Page 797-804, Year 2025
Publish date	Mar 12, 2025
Authors	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 / Minrui Fan /
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 ...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.
External links	Nature / PubMed:40074904
Methods	EM (single particle)
Resolution	2.72 - 2.9 Å
Structure data	61117 9j3j EMDB-61117, PDB-9j3j: Arabidopsis ATP/ADP translocator AtNTT1 Method: EM (single particle) / Resolution: 2.83 Å 61118 9j3l EMDB-61118, PDB-9j3l: ATP bound Arabidopsis ATP/ADP translocator AtNTT1 Method: EM (single particle) / Resolution: 2.72 Å 61119 9j3m EMDB-61119, PDB-9j3m: ADP/Pi bound Arabidopsis ATP/ADP translocator AtNTT1 Method: EM (single particle) / Resolution: 2.77 Å 61120 9j3n EMDB-61120, PDB-9j3n: ATP bound Chlamydia pneumoniae ATP/ADP translocator NTT1(Inward open state) Method: EM (single particle) / Resolution: 2.72 Å 61121 9j3o EMDB-61121, PDB-9j3o: Chlamydia pneumoniae ATP/ADP translocator NTT1(Outward open state) Method: EM (single particle) / Resolution: 2.9 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-PO4: PHOSPHATE ION
Source	Arabidopsis (plant) arabidopsis thaliana (thale cress) vicugna pacos (alpaca) chlamydia pneumoniae (bacteria)
Keywords	MEMBRANE PROTEIN / ATP/ADP translocator;non-mitochondrial;antiporter