Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli.
about
Essential cysteine residues of the type IIa Na+/Pi cotransporterIntragenic 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 siteA mutation in the Escherichia coli F0F1-ATP synthase rotor, gammaE208K, perturbs conformational coupling between transport and catalysis.36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase.Directed evolution of P-glycoprotein cysteines reveals site-specific, non-conservative substitutions that preserve multidrug resistance.The regulatory switch of F1-ATPase studied by single-molecule FRET in the ABEL Trap.Inter-subunit rotation and elastic power transmission in F0F1-ATPase.Chemical reactivities of cysteine substitutions in subunit a of ATP synthase define residues gating H+ transport from each side of the membrane.The torque of rotary F-ATPase can unfold subunit gamma if rotor and stator are cross-linked.Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane.Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase.Regulatory conformational changes of the ε subunit in single FRET-labeled FoF1-ATP synthase.The cytoplasmic loops of subunit a of Escherichia coli ATP synthase may participate in the proton translocating mechanism.Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: angular torque profile of the enzyme.Individual interactions of the b subunits within the stator of the Escherichia coli ATP synthaseEngineering a light-controlled F1 ATPase using structure-based protein design.Time-delayed in vivo assembly of subunit a into preformed Escherichia coli FoF1 ATP synthase.The proton-translocating a subunit of F0F1-ATP synthase is allocated asymmetrically to the peripheral stalk.F-ATPase: forced full rotation of the rotor despite covalent cross-link with the stator.F1-ATPase, the C-terminal end of subunit gamma is not required for ATP hydrolysis-driven rotation.Aqueous access channels in subunit a of rotary ATP synthase.The role of the epsilon subunit in the Escherichia coli ATP synthase. The C-terminal domain is required for efficient energy coupling.Fluidity of structure and swiveling of helices in the subunit c ring of Escherichia coli ATP synthase as revealed by cysteine-cysteine cross-linking.Rotation of the c subunit oligomer in EF(0)EF(1) mutant cD61N.Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5.Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle.
P2860
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P2860
Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli.
description
1998 nî lūn-bûn
@nan
1998 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli.
@ast
Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli.
@en
type
label
Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli.
@ast
Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli.
@en
prefLabel
Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli.
@ast
Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli.
@en
P2093
P2860
P1433
P1476
Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli.
@en
P2093
P2860
P304
P356
10.1016/S0014-5793(98)00337-8
P407
P577
1998-04-01T00:00:00Z