4.8 Article

Bacterial F-type ATP synthases follow a well-choreographed assembly pathway

Related references

Note: Only part of the references are listed.
Article Biochemistry & Molecular Biology

A systematic assessment of mycobacterial F1-ATPase subunit ε's role in latent ATPase hydrolysis

Chui-Fann Wong et al.

Summary: The mycobacterial F1FO-ATP synthase behaves differently from most bacteria due to the lack of ATP hydrolysis-driven proton translocation. Research on the central stalk subunit e has revealed its role in suppressing the enzyme's ATPase activity, providing insights for developing inhibitors targeting this subunit. By studying mutations at both the N-terminal and C-terminal of subunit epsilon, key residues important for the enzyme's function have been identified, paving the way for potential drug development targeting the F-ATP synthase.

FEBS JOURNAL (2021)

Article Biochemical Research Methods

LILBID and nESI: Different Native Mass Spectrometry Techniques as Tools in Structural Biology

Oliver Peetz et al.

JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY (2019)

Article Biochemistry & Molecular Biology

Molecular architecture of the N-type ATPase rotor ring from Burkholderia pseudomallei

Sarah Schulz et al.

EMBO REPORTS (2017)

Article Biochemistry & Molecular Biology

The stimulating role of subunit F in ATPase activity inside the A1-complex of the Methanosarcina mazei Go1 A1Ao ATP synthase

Dhirendra Singh et al.

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS (2016)

Article Biochemistry & Molecular Biology

Mitochondrial ATP synthase activity is impaired by suppressed O-GlcNAcylation in Alzheimer's disease

Moon-Yong Cha et al.

HUMAN MOLECULAR GENETICS (2015)

Article Biochemistry & Molecular Biology

Structural Basis for a Unique ATP Synthase Core Complex from Nanoarcheaum equitans

Soumya Mohanty et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2015)

Article Biochemistry & Molecular Biology

Assembly of the Escherichia coli FoF1 ATP synthase involves distinct subcomplex formation

Gabriele Deckers-Hebestreit

BIOCHEMICAL SOCIETY TRANSACTIONS (2013)

Article Multidisciplinary Sciences

Electric Field Driven Torque in ATP Synthase

John H. Miller et al.

PLOS ONE (2013)

Article Biochemistry & Molecular Biology

Modular assembly of yeast mitochondrial ATP synthase

Malgorzata Rak et al.

EMBO JOURNAL (2011)

Article Microbiology

Constant c10 Ring Stoichiometry in the Escherichia coli ATP Synthase Analyzed by Cross-Linking

Britta Ballhausen et al.

JOURNAL OF BACTERIOLOGY (2009)

Article Biochemistry & Molecular Biology

Chaperones of F1-ATPase

Anthony Ludlam et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2009)

Article Biochemistry & Molecular Biology

A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910

Marc R. de Jonge et al.

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2007)

Article Biochemistry & Molecular Biology

The role of subunit epsilon in the catalysis and regulation of FOF1-ATP synthase

Boris A. Feniouk et al.

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS (2006)

Article Biochemistry & Molecular Biology

Isolated ε subunit of Bacillus subtilis F1-ATPase binds ATP

Y Kato-Yamada

FEBS LETTERS (2005)

Article Biochemistry & Molecular Biology

The c15 ring of the Spirulina platensis F-ATP synthase:: F1/F0 symmetry mismatch is not obligatory

D Pogoryelov et al.

EMBO REPORTS (2005)

Article Biochemistry & Molecular Biology

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase

Z Ahmad et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2005)

Article Biochemistry & Molecular Biology

Assembly factors of F1F0-ATP synthase across genomes

A Pícková et al.

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2005)

Article Biochemistry & Molecular Biology

Involvement of ATP synthase residues αArg-376, βArg-182, and βLys-155 in Pi binding

Z Ahmad et al.

FEBS LETTERS (2005)

Article Multidisciplinary Sciences

A diarylquinoline drug active on the ATP synthase of Mycobacterium tuberculosis

K Andries et al.

SCIENCE (2005)

Article Multidisciplinary Sciences

Thermophilic ATP synthase has a decamer c-ring:: Indication of noninteger 10:3 H+/ATP ratio and permissive elastic coupling

N Mitome et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2004)

Article Biochemistry & Molecular Biology

Mutagenesis of residue βArg-246 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase

Z Ahmad et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2004)

Article Biochemistry & Molecular Biology

Mitochondrial diseases and ATPase defects of nuclear origin

J Houstek et al.

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS (2004)

Article Biochemistry & Molecular Biology

Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)

JA Leyva et al.

MOLECULAR MEMBRANE BIOLOGY (2003)

Article Biochemistry & Molecular Biology

Atp11p and Atp12p are chaperones for F1-ATPase biogenesis in mitochondria

SH Ackerman

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS (2002)

Article Multidisciplinary Sciences

Large conformational changes of the ε subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme

SP Tsunoda et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2001)

Article Multidisciplinary Sciences

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

WP Jiang et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2001)