ATP synthases: structure, function and evolution of unique energy converters
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A-, F- and V-adenosine 5'-triphosphatases (ATPases) consist of a mosaic of globular structural units which serve as functional units. These ion-translocating ATPases are thought to use a common mechanism to couple energy of ATP hydrolysis to ion transport and thus create an electrochemical ion gradient across the membrane. In vitro, all of these large protein complexes are able to use an ion gradient and the associated membrane potential to synthesize ATP. A-/F-/V-type ATPases are composed of two distinct segments: a catalytic sector, A1/F1/V1, whose three-dimensional structural relationship will be reviewed, and the membrane-embedded sector, Ao/Fo/Vo, which functions in ion conduction. Recent studies on the molecular biology of the Ao/Fo/Vo domains revealed surprising findings about duplicated and triplicated versions of the proteolipid subunit and shed new light on the evolution of these ion pumps.
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The catalytic and non-catalytic subunits of the ATP synthase R1 component are paralogs that arose prior to LUCA through an ancient duplication of a RecA family protein (P-loop NTPase) followed by loss of catalytic function in one subunit.
“The catalytic and non-catalytic subunits comprising the soluble hetero-hexameric R1 component, are paralogs to each other. They arose prior to LUCA through an ancient duplication of a RecA family protein (P-loop NTPase) followed by the loss of the catalytic function in one subunit”
From ATP synthase evolution on a cross-braced dated tree of life (2023) · cites this paper as [38]
Archaea and Bacteria contain primarily A/V-type and F-type ATP synthase subunits, respectively, and eukaryotes harbor complexes of both types.
“Archaea and Bacteria contain primarily A/V-type and F-type subunits, respectively, and eukaryotes harbor complexes of both types”
From ATP synthase evolution on a cross-braced dated tree of life (2023) · cites this paper as [38]
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References 131 · Cited by 174
- Authors
- M�ller, V., & Gr�ber, G.
- Affiliations
- Ludwig-Maximilians-Universität München (DE)
- Saarland University (DE)
- Venue
- Cellular and Molecular Life Sciences (CMLS)
- Published
- 2003-03-01
- Volume
- 60
- Issue
- 3
- Pages
- 474-494
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC11138706
- OpenAlex
- W2321770352
- Cited by
- 174
- References
- 131
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 3 · 2023: 5 · 2022: 5 · 2021: 7 · 2020: 9 · 2019: 5 · 2018: 7 · 2017: 7 · 2016: 4 · 2015: 8 · 2014: 4 · 2013: 9 · 2012: 5
- FWCI
- 4.14
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Health Assistance Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Keywords
- ATP synthase, F-ATPase, V-ATPase, ATP hydrolysis, ion transport, electrochemical gradient, membrane potential, protein evolution, ATP production
- MeSH terms
- Adenosine Triphosphate, Animals, Archaea, Bacteria, Cattle, Protein Binding, Bacterial Physiological Phenomena, Evolution, Molecular, Mitochondrial Proton-Translocating ATPases
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