ArticleJournal of molecular biology2014
NMR structures of α-proteobacterial ATPase-regulating ζ-subunits.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Inhibitory to non-inhibitory evolution of theFrontiers in molecular biosciences · 2023Article
- Evolution of the Inhibitory and Non-Inhibitory ε, ζ, and IFMicroorganisms · 2022Review
- The 3 × 120° rotary mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Control of rotation of the FJournal of bioenergetics and biomembranes · 2018Review
- Insights into the regulatory function of theOpen biology · 2018Review
- Deleting the IFOpen biology · 2018Article
- NMR in structural genomics to increase structural coverage of the protein universe: Delivered by Prof. Kurt Wüthrich on 7 July 2013 at the 38th FEBS Congress in St. Petersburg, Russia.The FEBS journal · 2016Article
- Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Inhibitory Mechanism of the ζ Subunit of the F1FO-ATPase Nanomotor of Paracoccus denitrificans and Related α-Proteobacteria.The Journal of biological chemistry · 2016Article
- Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structure of a catalytic dimer of the α- and β-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Purification, characterization and crystallization of the F-ATPase from Paracoccus denitrificans.Open biology · 2015Article
- J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4.Journal of biomolecular NMR · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
NMR structures of ζ-subunits, which are recently discovered α-proteobacterial F1F0-ATPase-regulatory proteins representing a Pfam protein family of 246 sequences from 219 species (PF07345), exhibit a four-helix bundle, which is different from all other known F1F0-ATPase inhibitors. Chemical shift mapping reveals a conserved ADP/ATP binding site in ζ-subunit, which mediates long-range conformational changes related to function, as revealed by the structure of the Paracoccus denitrificans ζ-subunit in complex with ADP. These structural data suggest a new mechanism of F1F0-ATPase regulation in α-proteobacteria.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.