The Molecular Basis for Purine Binding Selectivity in the Bacterial ATP Synthase ϵ Subunit-Reference-Cited by-同舟云学术

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The Molecular Basis for Purine Binding Selectivity in the Bacterial ATP Synthase ϵ Subunit

Published:2020-08-04 Issue:22 Volume:21 Page:3249-3254
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Krah Alexander¹²^ORCID,Huber Roland G.¹^ORCID,McMillan Duncan G. G.³^ORCID,Bond Peter J.¹⁴^ORCID

Affiliation:

1. Bioinformatics Institute Agency for Science, Technology and Research (A*STAR) 30 Biopolis Str. #07-01 Matrix Singapore 138671 Singapore

2. Korea Institute for Advanced Study School of Computational Sciences 85 Hoegiro Dongdaemun-gu, Seoul 02455 Republic of Korea

3. Delft University of Technology Department of Biotechnology Van der Maasweg 9 Delft 2629HZ The Netherlands

4. National University of Singapore Department of Biological Sciences 14 Science Drive 4 Singapore 117543 Singapore

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.202000291

Reference66 articles.

1. Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase

2. Direct observation of the rotation of F1-ATPase

3. A Specific Adaptation in the a Subunit of Thermoalkaliphilic F1FO-ATP Synthase Enables ATP Synthesis at High pH but Not at Neutral pH Values

4. Biophysical Characterization of a Thermoalkaliphilic Molecular Motor with a High Stepping Torque Gives Insight into Evolutionary ATP Synthase Adaptation

5. Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase

Cited by 5 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. ATP binding by an F1Fo ATP synthase ε subunit is pH dependent, suggesting a diversity of ε subunit functional regulation in bacteria;Frontiers in Molecular Biosciences;2023-02-27

2. Changes within the central stalk of E. coli F1Fo ATP synthase observed after addition of ATP;Communications Biology;2023-01-11

3. Atomic solution structure of Mycobacterium abscessus F‐ATP synthase subunit ε and identification of Ep1 Mab F1 as a targeted inhibitor;The FEBS Journal;2022-06-05

4. A second shell residue modulates a conserved ATP-binding site with radically different affinities for ATP;Biochimica et Biophysica Acta (BBA) - General Subjects;2021-01

5. Subunit epsilon of E. coli F1Fo ATP synthase attenuates enzyme activity by modulating central stalk flexibility;2020-09-30

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