Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
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The alpha- and beta-subunits of membrane-bound ATP synthase complex bind ATP and ADP: beta contributes to catalytic sites, and alpha may be involved in regulation of ATP synthase activity. The sequences of beta-subunits are highly conserved in Escherichia coli and bovine mitochondria. Also alpha and beta are weakly homologous to each other throughout most of their amino acid sequences, suggesting that they have common functions in catalysis. Related sequences in both alpha and beta and in other enzymes that bind ATP or ADP in catalysis, notably myosin, phosphofructokinase, and adenylate kinase, help to identify regions contributing to an adenine nucleotide binding fold in both ATP synthase subunits.
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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 [43]
There are only two basic ways that cells conserve energy as high energy phosphate bonds: substrate level phosphorylation and chemiosmotic energy harnessing using a rotor-stator ATP synthase.
“There are only two basic ways that cells conserve energy as high energy phosphate bonds: substrate level phosphorylation (Decker et al., 1970) and chemiosmotic energy harnessing using a rotor-stator ATP synthase (Walker et al., 1982; Walker, 2013).”
From Serpentinization as the source of energy, electrons, organics, catalysts, nutrients and pH gradients for the origin of LUCA and life (2023) · cites this paper as Walker et al., 1982
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- Authors
- Walker, J. E., Saraste, M., Runswick, M. J., & Gay, N. J.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Venue
- The EMBO Journal
- Published
- 1982-08-01
- Volume
- 1
- Issue
- 8
- Pages
- 945-951
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC553140
- OpenAlex
- W124504601
- Cited by
- 5,312
- References
- 0
- Citations by year
- 2026: 45 · 2025: 49 · 2024: 49 · 2023: 69 · 2022: 72 · 2021: 83 · 2020: 99 · 2019: 82 · 2018: 67 · 2017: 75 · 2016: 97 · 2015: 95 · 2014: 120 · 2013: 95 · 2012: 122
- FWCI
- 14.30
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Medical Research Council
- 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 › Protein Structure and Dynamics
- Keywords
- ATP synthase, alpha subunit, beta subunit, myosin, kinases, sequence homology, adenine nucleotide binding, phosphofructokinase, adenylate kinase, mitochondrial ATP synthase, Escherichia coli, bovine mitochondria, enzyme catalysis
- MeSH terms
- Mitochondrial ADP, ATP Translocases, Adenosine Diphosphate, Adenosine Triphosphate, Adenylate Kinase, Amino Acid Sequence, Animals, Binding Sites, Cattle, Escherichia coli, Mitochondria, Heart, Multienzyme Complexes, Myosins, Phosphofructokinase-1, Phosphotransferases, Protein Binding, Rabbits, Species Specificity, Submitochondrial Particles, ATP Synthetase Complexes, Macromolecular Substances
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