Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking.
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Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthaseStructure 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 SynthaseStructure-based design of a disulfide-linked oligomeric form of the simian virus 40 (SV40) large T antigen DNA-binding domainStructure of the rotor ring modified with N,N'-dicyclohexylcarbodiimide of the Na+-transporting vacuolar ATPaseThe F(0)F(1)-ATP synthase complex contains novel subunits and is essential for procyclic Trypanosoma bruceiCryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational statesMembrane embedded location of Na+ or H+ binding sites on the rotor ring of F1F0 ATP synthases.Arginine-induced conformational change in the c-ring/a-subunit interface of ATP synthase.Membrane topography of the coupling ion binding site in Na+-translocating F1F0 ATP synthase.Torque generation by the Fo motor of the sodium ATPase.Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: functional interactions between residues in the proton transport siteSubunit A of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent.Interaction of transmembrane helices in ATP synthase subunit a in solution as revealed by spin label difference NMR.ATP-driven stepwise rotation of FoF1-ATP synthase.Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation.Vanadate trapping of nucleotide at the ATP-binding sites of human multidrug resistance P-glycoprotein exposes different residues to the drug-binding siteMefloquine and new related compounds target the F(0) complex of the F(0)F(1) H(+)-ATPase of Streptococcus pneumoniae.Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase.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.Mechanics of coupling proton movements to c-ring rotation in ATP synthase.Structural study on the architecture of the bacterial ATP synthase Fo motor.Chemical reactivities of cysteine substitutions in subunit a of ATP synthase define residues gating H+ transport from each side of the membrane.Polar residues drive association of polyleucine transmembrane helicesDirect observation of stepped proteolipid ring rotation in E. coli F₀F₁-ATP synthase.High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na⁺-coupled ATP synthaseInteracting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm.Genetic and biochemical characterization of the F-ATPase operon from Streptococcus sanguis 10904.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.ATP synthesis without R210 of subunit a in the Escherichia coli ATP synthase.A conserved asparagine in a P-type proton pump is required for efficient gating of protons.Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane.Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthaseObstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase.A more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli 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.Structural divergence of the rotary ATPases.Twisting and subunit rotation in single F(O)(F1)-ATP synthase.
P2860
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P2860
Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Interacting helical faces of s ...... ed by disulfide cross-linking.
@ast
Interacting helical faces of s ...... ed by disulfide cross-linking.
@en
type
label
Interacting helical faces of s ...... ed by disulfide cross-linking.
@ast
Interacting helical faces of s ...... ed by disulfide cross-linking.
@en
prefLabel
Interacting helical faces of s ...... ed by disulfide cross-linking.
@ast
Interacting helical faces of s ...... ed by disulfide cross-linking.
@en
P2860
P356
P1476
Interacting helical faces of s ...... ed by disulfide cross-linking.
@en
P2093
R H Fillingame
P2860
P304
P356
10.1073/PNAS.95.12.6607
P407
P577
1998-06-01T00:00:00Z