ArticleOpen biology2015
Purification, characterization and crystallization of the F-ATPase from Paracoccus denitrificans.
Article in Open biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- The biogenesis and regulation of the plant oxidative phosphorylation system.Plant physiology · 2023Review
- FInternational journal of molecular sciences · 2023Review
- ATP synthase FCellular and molecular life sciences : CMLS · 2022Review
- The assembly, regulation and function of the mitochondrial respiratory chain.Nature reviews. Molecular cell biology · 2022Review
- Molecular Basis of the Pathogenic Mechanism Induced by the m.9191T>C Mutation in MitochondrialInternational journal of molecular sciences · 2020Article
- Dietary restriction protects from age-associated DNA methylation and induces epigenetic reprogramming of lipid metabolism.Genome biology · 2017Article
- Cardiolipin binds selectively but transiently to conserved lysine residues in the rotor of metazoan ATP synthases.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The structures of F-ATPases have been determined predominantly with mitochondrial enzymes, but hitherto no F-ATPase has been crystallized intact. A high-resolution model of the bovine enzyme built up from separate sub-structures determined by X-ray crystallography contains about 85% of the entire complex, but it lacks a crucial region that provides a transmembrane proton pathway involved in the generation of the rotary mechanism that drives the synthesis of ATP. Here the isolation, characterization and crystallization of an integral F-ATPase complex from the α-proteobacterium Paracoccus denitrificans are described. Unlike many eubacterial F-ATPases, which can both synthesize and hydrolyse ATP, the P. denitrificans enzyme can only carry out the synthetic reaction. The mechanism of inhibition of its ATP hydrolytic activity involves a ζ inhibitor protein, which binds to the catalytic F₁-domain of the enzyme. The complex that has been crystallized, and the crystals themselves, contain the nine core proteins of the complete F-ATPase complex plus the ζ inhibitor protein. The formation of crystals depends upon the presence of bound bacterial cardiolipin and phospholipid molecules; when they were removed, the complex failed to crystallize. The experiments open the way to an atomic structure of an F-ATPase complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.