ArticleThe Journal of biological chemistry2009
Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Functional importance of αAsp-350 in the catalytic sites of Escherichia coli ATP synthase.Archives of biochemistry and biophysics · 2019Article
- Energy metabolism controls phenotypes by protein efficiency and allocation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase.Archives of biochemistry and biophysics · 2016Article
- Asp residues of βDELSEED-motif are required for peptide binding in the Escherichia coli ATP synthase.International journal of biological macromolecules · 2015Article
- Article
- 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
- Rate of hydrolysis in ATP synthase is fine-tuned by α-subunit motif controlling active site conformation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- An alternative role of FoF1-ATP synthase in Escherichia coli: synthesis of thiamine triphosphate.Scientific reports · 2013Article
- ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptides.Current medicinal chemistry · 2013Review
- Two ATPases.The Journal of biological chemistry · 2012Review
- Effect of structural modulation of polyphenolic compounds on the inhibition of Escherichia coli ATP synthase.International journal of biological macromolecules · 2012Article
- Residue propensities, discrimination and binding site prediction of adenine and guanine phosphates.BMC biochemistry · 2011Article
- Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase.Journal of amino acids · 2011Article
- Dietary bioflavonoids inhibit Escherichia coli ATP synthase in a differential manner.International journal of biological macromolecules · 2010Article
- Inhibition of Escherichia coli ATP synthase by amphibian antimicrobial peptides.International journal of biological macromolecules · 2010Article
- The effect of NBD-Cl in nucleotide-binding of the major subunit alpha and B of the motor proteins F1FO ATP synthase and A1AO ATP synthase.Journal of bioenergetics and biomembranes · 2010Article
- Medicinal chemistry of ATP synthase: a potential drug target of dietary polyphenols and amphibian antimicrobial peptides.Current medicinal chemistry · 2010Review
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
This paper describes the role of alpha-subunit VISIT-DG sequence residues alphaSer-347 and alphaGly-351 in catalytic sites of Escherichia coli F(1)F(o) ATP synthase. X-ray structures show the very highly conserved alpha-subunit VISIT-DG sequence in close proximity to the conserved phosphate-binding residues alphaArg-376, betaArg-182, betaLys-155, and betaArg-246 in the phosphate-binding subdomain. Mutations alphaS347Q and alphaG351Q caused loss of oxidative phosphorylation and reduced ATPase activity of F(1)F(o) in membranes by 100- and 150-fold, respectively, whereas alphaS347A mutation showed only a 13-fold loss of activity and also retained some oxidative phosphorylation activity. The ATPase of alphaS347Q mutant was not inhibited, and the alphaS347A mutant was slightly inhibited by MgADP-azide, MgADP-fluoroaluminate, or MgADP-fluoroscandium, in contrast to wild type and alphaG351Q mutant. Whereas 7-chloro-4-nitrobenzo-2-oxa-1, 3-diazole (NBD-Cl) inhibited wild type and alphaG351Q mutant ATPase essentially completely, ATPase in alphaS347A or alphaS347Q mutant was inhibited maximally by approximately 80-90%, although reaction still occurred at residue betaTyr-297, proximal to the alpha-subunit VISIT-DG sequence, near the phosphate-binding pocket. Inhibition characteristics supported the conclusion that NBD-Cl reacts inbetaE (empty) catalytic sites, as shown previously by x-ray structure analysis. Phosphate protected against NBD-Cl inhibition in wild type and alphaG351Q mutant but not in alphaS347Q or alphaS347A mutant. The results demonstrate that alphaSer-347 is an additional residue involved in phosphate-binding and transition state stabilization in ATP synthase catalytic sites. In contrast, alphaGly-351, although strongly conserved and clearly important for function, appears not to play a direct role.
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