Defining the domain of binding of F1 subunit epsilon with the polar loop of F0 subunit c in the Escherichia coli ATP synthase (Q77841244)

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8 December 2019

title

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

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8 December 2019

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3

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8 December 2019

author name string

J Hermolin

series ordinal

1

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8 December 2019

O Y Dmitriev

series ordinal

2

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8 December 2019

R H Fillingame

series ordinal

4

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8 December 2019

language of work or name

English

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publication date

1 June 1999

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Journal of Biological Chemistry

8 December 2019

number of pages

6

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based on heuristic

inferred from page(s)

published in

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8 December 2019

volume

274

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8 December 2019

issue

24

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8 December 2019

page(s)

17011-17016

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Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase

8 December 2019

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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

21 January 2018

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

21 January 2018

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ATP Synthesis by Rotary Catalysis (Nobel lecture)

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Direct observation of the rotation of F1-ATPase

21 January 2018

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F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps

21 January 2018

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

21 January 2018

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

21 January 2018

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Rotation of the epsilon subunit during catalysis by Escherichia coli FOF1-ATP synthase

21 January 2018

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Intersubunit rotation in active F-ATPase

21 January 2018

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Three-stepped rotation of subunits gamma and epsilon in single molecules of F-ATPase as revealed by polarized, confocal fluorometry

21 January 2018

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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.

21 January 2018

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Cross-linking of chloroplast F0F1-ATPase subunit epsilon to gamma without effect on activity. Epsilon and gamma are parts of the rotor

21 January 2018

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

21 January 2018

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

21 January 2018

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The essential arginine residue at position 210 in the alpha subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity

21 January 2018

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On the role of Arg-210 and Glu-219 of subunit a in proton translocation by the Escherichia coli F0F1-ATP synthase

21 January 2018

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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

21 January 2018

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ATP synthase's second stalk comes into focus

21 January 2018

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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.

21 January 2018

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The gamma subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 part

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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ATP synthase: a tentative structural model

21 January 2018

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Energy transduction in ATP synthase

21 January 2018

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Characterization of a b2delta complex from Escherichia coli ATP synthase

21 January 2018

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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

21 January 2018

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Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase

21 January 2018

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

21 January 2018

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

21 January 2018

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The UNC operon nucleotide sequence, regulation and structure of ATP-synthase

21 January 2018

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

21 January 2018

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Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

21 January 2018

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Organization of the F0 sector of Escherichia coli H+-ATPase: the polar loop region of subunit c extends from the cytoplasmic face of the membrane

21 January 2018

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Monoclonal antibody modification of the ATPase activity of Escherichia coli F1 ATPase.

21 January 2018

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Arrangement of the epsilon subunit in the Escherichia coli ATP synthase from the reactivity of cysteine residues introduced at different positions in this subunit.

21 January 2018

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Mutations at Glu-32 and His-39 in the epsilon subunit of the Escherichia coli F1F0 ATP synthase affect its inhibitory properties.

21 January 2018

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Interactions between the F1 and F0 parts in the Escherichia coli ATP synthase. Associations involving the loop region of C subunits.

21 January 2018

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F1-ATPase: a rotary motor made of a single molecule

21 January 2018

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Energy transduction in the F1 motor of ATP synthase

21 January 2018

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The coupling region of F0F1 ATP synthase: binding of the hydrophilic loop of F0 subunit c to F1

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.274.24.17011

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10358051%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

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