ArticleJournal of amino acids2011
Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase.
Article in Journal of amino acids, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Integrated Experimental and Computational Investigation of Azobenzenoid Derivatives Against Trypanosomatid: RNA Editing Ligase 1 as a Potential Molecular Target.Acta parasitologica · 2026Article
- The molecular mechanism of ATP synthase constrains the evolutionary landscape of chemiosmosis.Biophysical journal · 2025Review
- Electric Forces and ATP Synthesis.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Identification of structural motifs critical for human G6PC2 function informed by sequence analysis and an AlphaFold2-predicted model.Bioscience reports · 2024Article
- Functional importance of αAsp-350 in the catalytic sites of Escherichia coli ATP synthase.Archives of biochemistry and biophysics · 2019Article
- A Therapeutic Connection between Dietary Phytochemicals and ATP Synthase.Current medicinal chemistry · 2017Review
- Understanding the link between antimicrobial properties of dietary olive phenolics and bacterial ATP synthase.International journal of biological macromolecules · 2017Article
- Safranal and its analogs inhibit Escherichia coli ATP synthase and cell growth.International journal of biological macromolecules · 2017Article
- Asp residues of βDELSEED-motif are required for peptide binding in the Escherichia coli ATP synthase.International journal of biological macromolecules · 2015Article
- Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.Biochemistry · 2014Article
- ATP synthase: the right size base model for nanomotors in nanomedicine.TheScientificWorldJournal · 2014Review
- ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptides.Current medicinal chemistry · 2013Review
- Effect of structural modulation of polyphenolic compounds on the inhibition of Escherichia coli ATP synthase.International journal of biological macromolecules · 2012Article
- Rational engineering of enzyme allosteric regulation through sequence evolution analysis.PLoS computational biology · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Here we describe the role of charged amino acids at the catalytic sites of Escherichia coli ATP synthase. There are four positively charged and four negatively charged residues in the vicinity of of E. coli ATP synthase catalytic sites. Positive charges are contributed by three arginine and one lysine, while negative charges are contributed by two aspartic acid and two glutamic acid residues. Replacement of arginine with a neutral amino acid has been shown to abrogate phosphate binding, while restoration of phosphate binding has been accomplished by insertion of arginine at the same or a nearby location. The number and position of positive charges plays a critical role in the proper and efficient binding of phosphate. However, a cluster of many positive charges inhibits phosphate binding. Moreover, the presence of negatively charged residues seems a requisite for the proper orientation and functioning of positively charged residues in the catalytic sites. This implies that electrostatic interactions between amino acids are an important constituent of initial phosphate binding in the catalytic sites. Significant loss of function in growth and ATPase activity assays in mutants generated through charge modulations has demonstrated that precise location and stereochemical interactions are of paramount importance.
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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.