Cooperative three-step motions in catalytic subunits of F(1)-ATPase correlate with 80 degrees and 40 degrees substep rotations (Q82619781)

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17 January 2020

title

Cooperative three-step motions in catalytic subunits of F(1)-ATPase correlate with 80 degrees and 40 degrees substep rotations (English)

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17 January 2020

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17 January 2020

author name string

Tomoko Masaike

1

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17 January 2020

Fumie Koyama-Horibe

2

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17 January 2020

Masasuke Yoshida

4

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17 January 2020

Takayuki Nishizaka

5

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17 January 2020

publication date

16 November 2008

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Nature Structural & Molecular Biology

17 January 2020

number of pages

8

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inferred from page(s)

published in

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17 January 2020

volume

15

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issue

12

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page(s)

1326-1333

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https://scigraph.springernature.com/pub.10.1038/nsmb.1510

17 January 2020

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cites work

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

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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase

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Catalysis and rotation of F1 motor: cleavage of ATP at the catalytic site occurs in 1 ms before 40 degree substep rotation

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F1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits

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Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation

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Origin of apparent negative cooperativity of F(1)-ATPase

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The alpha3(betaMet222Ser/Tyr345Trp)3gamma subcomplex of the TF1-ATPase does not hydolyze ATP at a significant rate until the substrate binds to the catalytic site of the lowest affinity

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

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Oxidation of the alpha(3)(betaD311C/R333C)(3)gamma subcomplex of the thermophilic Bacillus PS3 F(1)-ATPase indicates that only two beta subunits can exist in the closed conformation simultaneously

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Cross-linking of two beta subunits in the closed conformation in F1-ATPase

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Probing conformations of the beta subunit of F0F1-ATP synthase in catalysis

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The energy transmission in ATP synthase: from the gamma-c rotor to the alpha 3 beta 3 oligomer fixed by OSCP-b stator via the beta DELSEED sequence

31 March 2020

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Single Molecule Dynamics Studied by Polarization Modulation

31 March 2020

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Spatial precision of a catalytic carboxylate of F1-ATPase beta subunit probed by introducing different carboxylate-containing side chains

31 March 2020

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Stepping rotation of F(1)-ATPase with one, two, or three altered catalytic sites that bind ATP only slowly

31 March 2020

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

31 March 2020

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The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin

31 March 2020

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The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B

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Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism

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Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride

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Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis

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Axle-less F1-ATPase rotates in the correct direction

31 March 2020

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Crystal structures of a multidrug transporter reveal a functionally rotating mechanism.

31 March 2020

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Structure of the whole cytosolic region of ATP-dependent protease FtsH.

31 March 2020

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Pause and rotation of F(1)-ATPase during catalysis

31 March 2020

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Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSMB.1510

1 reference

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17 January 2020

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