Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ (Q34985080)

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English	Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ	scientific article

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scholarly article

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Europe PubMed Central

5 August 2017

1 reference

Europe PubMed Central

Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ (English)

1 reference

Europe PubMed Central

5 August 2017

transmembrane transport

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transmembrane protein

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author name string

Robert H Fillingame

1

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Europe PubMed Central

5 August 2017

Oleg Y Dmitriev

2

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Europe PubMed Central

5 August 2017

language of work or name

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publication date

1 October 2002

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Europe PubMed Central

5 August 2017

Biochimica et Biophysica Acta

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Europe PubMed Central

5 August 2017

1565

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Europe PubMed Central

5 August 2017

2

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Europe PubMed Central

5 August 2017

232-245

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Europe PubMed Central

5 August 2017

ATP synthesis by oxidative phosphorylation

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The oligomeric subunit C rotor in the fo sector of ATP synthase: unresolved questions in our understanding of function

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The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10.

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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Intersubunit rotation in active F-ATPase

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Direct observation of the rotation of F1-ATPase

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ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis

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Characterization of the interface between gamma and epsilon subunits of Escherichia coli F1-ATPase

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Direct observation of the rotation of epsilon subunit in F1-ATPase

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Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation

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F-ATPase: specific observation of the rotating c subunit oligomer of EF(o)EF(1)

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Rotation of a complex of the gamma subunit and c ring of Escherichia coli ATP synthase. The rotor and stator are interchangeable

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Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase

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ATP synthase: a tentative structural model

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Energy transduction in ATP synthase

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Molecular imaging of Escherichia coli F0F1-ATPase in reconstituted membranes using atomic force microscopy

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Topographical structure of membrane-bound Escherichia coli F1F0 ATP synthase in aqueous buffer

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Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase

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Arrangement of the multicopy H+-translocating subunit c in the membrane sector of the Escherichia coli F1F0 ATP synthase.

1 reference

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7 January 2021

Genetic fusions of subunit c in the F0 sector of H+-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis

1 reference

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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

1 reference

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Subunits coupling H+ transport and ATP synthesis in the Escherichia coli ATP synthase. Cys-Cys cross-linking of F1 subunit epsilon to the polar loop of F0 subunit c.

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The stalk region of the Escherichia coli ATP synthase. Tyrosine 205 of the gamma subunit is in the interface between the F1 and F0 parts and can interact with both the epsilon and c oligomer.

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Defining the domain of binding of F1 subunit epsilon with the polar loop of F0 subunit c in the Escherichia coli ATP synthase

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Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy

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Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli

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Structure of the gamma-epsilon complex of ATP synthase

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Molecular architecture of the rotary motor in ATP synthase

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Structural biology. Proton-powered turbine of a plant motor

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Bacterial Na(+)-ATP synthase has an undecameric rotor

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Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking

1 reference

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Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase

1 reference

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The second stalk of Escherichia coli ATP synthase

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ATP synthase's second stalk comes into focus

1 reference

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Direct indication for the existence of a double stalk in CF 0 F 1 1 1Edited by J. Karn

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ATP Synthesis by Rotary Catalysis (Nobel lecture)

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Characterization of a b2delta complex from Escherichia coli ATP synthase

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The second stalk composed of the b- and delta-subunits connects F0 to F1 via an alpha-subunit in the Escherichia coli ATP synthase

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Disulfide linkage of the b and delta subunits does not affect the function of the Escherichia coli ATP synthase

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Insights into the rotary catalytic mechanism of F0F1 ATP synthase from the cross-linking of subunits b and c in the Escherichia coli enzyme

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Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase.

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Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues.

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A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase

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Structural changes linked to proton translocation by subunit c of the ATP synthase

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The essential carboxyl group in subunit c of the F1F0 ATP synthase can be moved and H(+)-translocating function retained

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The F1F0-ATPase of Escherichia coli. Substitution of proline by leucine at position 64 in the c-subunit causes loss of oxidative phosphorylation.

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Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices

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Hairpin folding of subunit c of F1Fo ATP synthase: 1H distance measurements to nitroxide-derivatized aspartyl-61.

1 reference

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Proton-translocating carboxyl of subunit c of F1Fo H(+)-ATP synthase: the unique environment suggested by the pKa determined by 1H NMR.

1 reference

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Changing the ion binding specificity of the Escherichia coli H(+)-transporting ATP synthase by directed mutagenesis of subunit c.

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Molecular basis for the coupling ion selectivity of F1F0 ATP synthases: probing the liganding groups for Na+ and Li+ in the c subunit of the ATP synthase from Propionigenium modestum.

1 reference

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Apoprotein structure in the LH2 complex from Rhodopseudomonas acidophila strain 10050: modular assembly and protein pigment interactions

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Electron-crystallographic refinement of the structure of bacteriorhodopsin

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Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex

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Operation of the F(0) motor of the ATP synthase

1 reference

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NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles

1 reference

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Model of the c-subunit oligomer in the membrane domain of F-ATPases.

1 reference

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Molecular architecture of the c-subunit oligomer in the membrane domain of F-ATPases probed by tryptophan substitution mutagenesis.

1 reference

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Molecular contacts in the transmembrane c-subunit oligomer of F-ATPases identified by tryptophan substitution mutagenesis

1 reference

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The gammaepsilon-c subunit interface in the ATP synthase of Escherichia coli. cross-linking of the epsilon subunit to the c subunit ring does not impair enzyme function, that of gamma to c subunits leads to uncoupling

1 reference

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Structure of Ala24/Asp61 --> Asp24/Asn61 substituted subunit c of Escherichia coli ATP synthase: implications for the mechanism of proton transport and rotary movement in the F0 complex

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Molecular rotary motors

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7 January 2021

Identifiers

10.1016/S0005-2736(02)00572-2

1 reference

Europe PubMed Central

5 August 2017

1 reference

Europe PubMed Central

5 August 2017

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