ArticleThe Journal of biological chemistry2008
Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Conformational ensemble of yeast ATP synthase at low pH reveals unique intermediates and plasticity in FNature structural & molecular biology · 2024Article
- Engineered Protein Model of the ATP synthase HScientific reports · 2018Article
- Analysis of an N-terminal deletion in subunit a of the Escherichia coli ATP synthase.Journal of bioenergetics and biomembranes · 2017Article
- Cryo-EM structures of the autoinhibitedeLife · 2016Article
- Structure and mechanism of the ATP synthase membrane motor inferred from quantitative integrative modeling.The Journal of general physiology · 2016Article
- Probing the proton channels in subunit N of Complex I from Escherichia coli through intra-subunit cross-linking.Biochimica et biophysica acta · 2016Article
- Regulation of Vacuolar H+-ATPase (V-ATPase) Reassembly by Glycolysis Flow in 6-Phosphofructo-1-kinase (PFK-1)-deficient Yeast Cells.The Journal of biological chemistry · 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
- Constraining the Lateral Helix of Respiratory Complex I by Cross-linking Does Not Impair Enzyme Activity or Proton Translocation.The Journal of biological chemistry · 2015Article
- Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase.Nature · 2015Article
- Fo-driven Rotation in the ATP Synthase Direction against the Force of F1 ATPase in the FoF1 ATP Synthase.The Journal of biological chemistry · 2015Article
- Understanding structure, function, and mutations in the mitochondrial ATP synthase.Microbial cell (Graz, Austria) · 2015Article
- Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Residues in the polar loop of subunit c in Escherichia coli ATP synthase function in gating proton transport to the cytoplasm.The Journal of biological chemistry · 2014Article
- Escherichia coli F1Fo-ATP synthase with a b/δ fusion protein allows analysis of the function of the individual b subunits.The Journal of biological chemistry · 2013Article
- Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase.The Journal of biological chemistry · 2013Article
- Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking.FEBS letters · 2013Article
- Structural study on the architecture of the bacterial ATP synthase Fo motor.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Cell-free synthesis of membrane subunits of ATP synthase in phospholipid bicelles: NMR shows subunit a fold similar to the protein in the cell membrane.Protein science : a publication of the Protein Society · 2012Article
- Interaction with monomeric subunit c drives insertion of ATP synthase subunit a into the membrane and primes a-c complex formation.The Journal of biological chemistry · 2011Article
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2 authors.
Funding
Abstract
Subunit a plays a key role in promoting H+ transport and the coupled rotary motion of the subunit c ring in F1F0-ATP synthase. H+ binding and release occur at Asp-61 in the middle of the second transmembrane helix (TMH) of F0 subunit c. H+ are thought to reach Asp-61 via aqueous pathways mapping to the surfaces of TMHs 2-5 of subunit a. TMH4 of subunit a is thought to pack close to TMH2 of subunit c based upon disulfide cross-link formation between Cys substitutions in both TMHs. Here we substituted Cys into the fifth TMH of subunit a and the second TMH of subunit c and tested for cross-linking using bis-methanethiosulfonate (bis-MTS) reagents. A total of 62 Cys pairs were tested and 12 positive cross-links were identified with variable alkyl length linkers. Cross-linking was achieved near the middle of the bilayer for the Cys pairs a248C/c62C, a248C/ c63C, a248C/c65C, a251C/c57C, a251C/c59C, a251C/c62C, a252C/c62C, and a252C/c65C. Cross-linking was achieved near the cytoplasmic side of the bilayer for Cys pairs a262C/c53C, a262C/c54C, a262C/c55C, and a263C/c54C. We conclude that both aTMH4 and aTMH5 pack proximately to cTMH2 of the c-ring. In other experiments we demonstrate that aTMH4 and aTMH5 can be simultaneously cross-linked to different subunit c monomers in the c-ring. Five mutants showed pH-dependent cross-linking consistent with aTMH5 changing conformation at lower pH values to facilitate cross-linking. We suggest that the pH-dependent conformational change may be related to the proposed role of aTMH5 in gating H+ access from the periplasm to the cAsp-61 residue in cTMH2.
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