ArticleThe Journal of biological chemistry2015
Crystal structure of subunits D and F in complex gives insight into energy transmission of the eukaryotic V-ATPase from Saccharomyces cerevisiae.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 41 citations in OpenAlex.
- Eukaryotic yeast VFrontiers in molecular biosciences · 2024Article
- Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Morphological and Genomic Features of the New Klosneuvirinae Isolate Fadolivirus IHUMI-VV54.Frontiers in microbiology · 2021Article
- Abundant neuroprotective chaperone Lipocalin-type prostaglandin D synthase (L-PGDS) disassembles the Amyloid-β fibrils.Scientific reports · 2019Article
- Pyrazinoic Acid Inhibits Mycobacterial Coenzyme A Biosynthesis by Binding to Aspartate Decarboxylase PanD.ACS infectious diseases · 2017Article
- The uniqueness of subunit α of mycobacterial F-ATP synthases: An evolutionary variant for niche adaptation.The Journal of biological chemistry · 2017Article
- Structural features of NS3 of Dengue virus serotypes 2 and 4 in solution and insight into RNA binding and the inhibitory role of quercetin.Acta crystallographica. Section D, Structural biology · 2017Article
- Breaking up and making up: The secret life of the vacuolar HProtein science : a publication of the Protein Society · 2017Review
- Essential role of the flexible linker on the conformational equilibrium of bacterial peroxiredoxin reductase for effective regeneration of peroxiredoxin.The Journal of biological chemistry · 2017Article
- Power Stroke Angular Velocity Profiles of Archaeal A-ATP Synthase Versus Thermophilic and Mesophilic F-ATP Synthase Molecular Motors.The Journal of biological chemistry · 2016Article
- Crystal structure of yeast V1-ATPase in the autoinhibited state.The EMBO journal · 2016Article
- Proton Transport and pH Control in Fungi.Advances in experimental medicine and biology · 2016Review
- Structural insight and flexible features of NS5 proteins from all four serotypes of Dengue virus in solution.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Recent Insights into the Structure, Regulation, and Function of the V-ATPases.Trends in biochemical sciences · 2015Review
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic V1VO-ATPases hydrolyze ATP in the V1 domain coupled to ion pumping in VO. A unique mode of regulation of V-ATPases is the reversible disassembly of V1 and VO, which reduces ATPase activity and causes silencing of ion conduction. The subunits D and F are proposed to be key in these enzymatic processes. Here, we describe the structures of two conformations of the subunit DF assembly of Saccharomyces cerevisiae (ScDF) V-ATPase at 3.1 Å resolution. Subunit D (ScD) consists of a long pair of α-helices connected by a short helix ((79)IGYQVQE(85)) as well as a β-hairpin region, which is flanked by two flexible loops. The long pair of helices is composed of the N-terminal α-helix and the C-terminal helix, showing structural alterations in the two ScDF structures. The entire subunit F (ScF) consists of an N-terminal domain of four β-strands (β1-β4) connected by four α-helices (α1-α4). α1 and β2 are connected via the loop (26)GQITPETQEK(35), which is unique in eukaryotic V-ATPases. Adjacent to the N-terminal domain is a flexible loop, followed by a C-terminal α-helix (α5). A perpendicular and extended conformation of helix α5 was observed in the two crystal structures and in solution x-ray scattering experiments, respectively. Fitted into the nucleotide-bound A3B3 structure of the related A-ATP synthase from Enterococcus hirae, the arrangements of the ScDF molecules reflect their central function in ATPase-coupled ion conduction. Furthermore, the flexibility of the terminal helices of both subunits as well as the loop (26)GQITPETQEK(35) provides information about the regulatory step of reversible V1VO disassembly.
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