Subunit a facilitates aqueous access to a membrane-embedded region of subunit c in Escherichia coli F1F0 ATP synthase.
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Structure of the c14 Rotor Ring of the Proton Translocating Chloroplast ATP SynthaseHigh-resolution structure of the rotor ring of a proton-dependent ATP synthaseStructure of the c10 ring of the yeast mitochondrial ATP synthase in the open conformationA new type of Na(+)-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motifCryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational statesF1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations.The ATP synthase a-subunit of extreme alkaliphiles is a distinct variant: mutations in the critical alkaliphile-specific residue Lys-180 and other residues that support alkaliphile oxidative phosphorylation.Chemical reactivities of cysteine substitutions in subunit a of ATP synthase define residues gating H+ transport from each side of the membrane.Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm.Electric field driven torque in ATP synthase.Definition of membrane topology and identification of residues important for transport in subunit a of the vacuolar ATPase.Promiscuous archaeal ATP synthase concurrently coupled to Na+ and H+ translocation.Cell-free synthesis of membrane subunits of ATP synthase in phospholipid bicelles: NMR shows subunit a fold similar to the protein in the cell membraneConstraining the Lateral Helix of Respiratory Complex I by Cross-linking Does Not Impair Enzyme Activity or Proton Translocation.Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase.Aqueous accessibility to the transmembrane regions of subunit c of the Escherichia coli F1F0 ATP synthase.Structure and mechanism of the ATP synthase membrane motor inferred from quantitative integrative modeling.Residues in the polar loop of subunit c in Escherichia coli ATP synthase function in gating proton transport to the cytoplasm.The c-Ring of the F1FO-ATP Synthase: Facts and Perspectives.Interaction with monomeric subunit c drives insertion of ATP synthase subunit a into the membrane and primes a-c complex formation.Predicted Structures of the Proton-Bound Membrane-Embedded Rotor Rings of the Saccharomyces cerevisiae and Escherichia coli ATP Synthases.Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linkingResolving the negative potential side (n-side) water-accessible proton pathway of F-type ATP synthase by molecular dynamics simulations.Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase.Probing the proton channels in subunit N of Complex I from Escherichia coli through intra-subunit cross-linking.Analysis of an N-terminal deletion in subunit a of the Escherichia coli ATP synthase.
P2860
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P2860
Subunit a facilitates aqueous access to a membrane-embedded region of subunit c in Escherichia coli F1F0 ATP synthase.
description
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name
Subunit a facilitates aqueous ...... richia coli F1F0 ATP synthase.
@en
Subunit a facilitates aqueous ...... richia coli F1F0 ATP synthase.
@nl
type
label
Subunit a facilitates aqueous ...... richia coli F1F0 ATP synthase.
@en
Subunit a facilitates aqueous ...... richia coli F1F0 ATP synthase.
@nl
prefLabel
Subunit a facilitates aqueous ...... richia coli F1F0 ATP synthase.
@en
Subunit a facilitates aqueous ...... richia coli F1F0 ATP synthase.
@nl
P2860
P356
P1476
Subunit a facilitates aqueous ...... erichia coli F1F0 ATP synthase
@en
P2093
Robert H Fillingame
P2860
P304
12365-12372
P356
10.1074/JBC.M800901200
P407
P50
P577
2008-03-10T00:00:00Z