Structure, mechanism, and regulation of the chloroplast ATP synthase.

TitleStructure, mechanism, and regulation of the chloroplast ATP synthase.
Publication TypeJournal Article
Year of Publication2018
AuthorsHahn, A, Vonck, J, Mills, DJ, Meier, T, Kühlbrandt, W
JournalScience
Volume360
Issue6389
Date Published2018 05 11
ISSN1095-9203
KeywordsAdenosine Triphosphate, Chloroplast Proton-Translocating ATPases, Chloroplasts, Cryoelectron Microscopy, Evolution, Molecular, Molecular Motor Proteins, Plant Leaves, Protein Conformation, Protein Subunits, Rotation, Spinacia oleracea
Abstract

The chloroplast adenosine triphosphate (ATP) synthase uses the electrochemical proton gradient generated by photosynthesis to produce ATP, the energy currency of all cells. Protons conducted through the membrane-embedded F motor drive ATP synthesis in the F head by rotary catalysis. We determined the high-resolution structure of the complete cFF complex by cryo-electron microscopy, resolving side chains of all 26 protein subunits, the five nucleotides in the F head, and the proton pathway to and from the rotor ring. The flexible peripheral stalk redistributes differences in torsional energy across three unequal steps in the rotation cycle. Plant ATP synthase is autoinhibited by a β-hairpin redox switch in subunit γ that blocks rotation in the dark.

DOI10.1126/science.aat4318
Alternate JournalScience
Citation Key10.1126/science.aat4318
PubMed ID29748256
Grant List / / Wellcome Trust / United Kingdom