Topographical structure of membrane-bound Escherichia coli F1F0 ATP synthase in aqueous buffer.
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Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthaseStructural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallographyStructure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helicesStructure of the c14 Rotor Ring of the Proton Translocating Chloroplast ATP SynthaseAssociation of the eukaryotic V1VO ATPase subunits a with d and d with A.Proton translocation driven by ATP hydrolysis in V-ATPasesMembrane embedded location of Na+ or H+ binding sites on the rotor ring of F1F0 ATP synthases.Membrane topography of the coupling ion binding site in Na+-translocating F1F0 ATP synthase.ATP-driven stepwise rotation of FoF1-ATP synthase.Subunit rotation of ATP synthase embedded in membranes: a or beta subunit rotation relative to the c subunit ring.Filipin-induced lesions in planar phospholipid bilayers imaged by atomic force microscopyATP synthase and other motor proteinsEnergy transduction in the sodium F-ATPase of Propionigenium modestum.Structure of the subunit c oligomer in the F1Fo ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme.Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking.Visualization of a peripheral stalk in V-type ATPase: evidence for the stator structure essential to rotational catalysis.Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthaseStochastic rotational catalysis of proton pumping F-ATPaseCharge displacements during ATP-hydrolysis and synthesis of the Na+-transporting FoF1-ATPase of Ilyobacter tartaricus.ATP synthase: a tentative structural model.Mode of interaction of the single a subunit with the multimeric c subunits during the translocation of the coupling ions by F1F0 ATPasesVoltage-generated torque drives the motor of the ATP synthase.F(0) of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring.Rotation of a complex of the gamma subunit and c ring of Escherichia coli ATP synthase. The rotor and stator are interchangeable.Aqueous access channels in subunit a of rotary ATP synthase.ATP-dependent rotation of mutant ATP synthases defective in proton transport.Arrangement of the multicopy H+-translocating subunit c in the membrane sector of the Escherichia coli F1F0 ATP synthase.Insertion scanning mutagenesis of subunit a of the F1F0 ATP synthase near His245 and implications on gating of the proton channel.Self-assembly of ATP synthase subunit c rings.Interactions between the F1 and F0 parts in the Escherichia coli ATP synthase. Associations involving the loop region of C subunits.Simulations of the c-subunit of ATP-synthase reveal helix rearrangements.Transient accumulation of elastic energy in proton translocating ATP synthase
P2860
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P2860
Topographical structure of membrane-bound Escherichia coli F1F0 ATP synthase in aqueous buffer.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Topographical structure of mem ...... TP synthase in aqueous buffer.
@en
type
label
Topographical structure of mem ...... TP synthase in aqueous buffer.
@en
prefLabel
Topographical structure of mem ...... TP synthase in aqueous buffer.
@en
P2093
P2860
P1433
P1476
Topographical structure of mem ...... TP synthase in aqueous buffer.
@en
P2093
P2860
P356
10.1016/S0014-5793(96)01127-1
P407
P577
1996-11-01T00:00:00Z