ArticleNature2012
Crystal structure of a membrane-embedded H+-translocating pyrophosphatase.
Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed.
- Conformational dynamics and asymmetry in multimodal inhibition of membrane-bound pyrophosphatases.eLife · 2025Article
- Revealing the glutamate switch: Insights into proton translocation in plant HBiophysical journal · 2025Article
- Systematic identification of sugarcane vacuolar HPlant cell reports · 2024Article
- NaInternational journal of molecular sciences · 2024Article
- Advances in the cellular biology, biochemistry, and molecular biology of acidocalcisomes.Microbiology and molecular biology reviews : MMBR · 2024Review
- Genome-Wide Identification of theInternational journal of molecular sciences · 2024Article
- Functional and structural asymmetry suggest a unifying principle for catalysis in membrane-bound pyrophosphatases.EMBO reports · 2024Article
- Exploration of the Catalytic Cycle Dynamics of Vigna Radiata HThe Journal of membrane biology · 2023Article
- Plasmodium falciparum utilizes pyrophosphate to fuel an essential proton pump in the ring stage and the transition to trophozoite stage.PLoS pathogens · 2023Article
- Phosphorus Chemistry at the Roots of Bioenergetics: Ligand Permutation as the Molecular Basis of the Mechanism of ATP Synthesis/Hydrolysis by FMolecules (Basel, Switzerland) · 2023Article
- Crystal structures of dimeric and heptameric mtHsp60 reveal the mechanism of chaperonin inactivation.Life science alliance · 2023Article
- HMicroorganisms · 2023Article
- Roles of type II HFrontiers in plant science · 2023Article
- A self-sustaining serpentinization mega-engine feeds the fougerite nanoengines implicated in the emergence of guided metabolism.Frontiers in microbiology · 2023Article
- Yeast as a tool for membrane protein production and structure determination.FEMS yeast research · 2022Article
- mPPases create a conserved anionic membrane fingerprint as identified via multi-scale simulations.PLoS computational biology · 2022Article
- Pre-steady-state kinetics and solvent isotope effects support the "billiard-type" transport mechanism in NaProtein science : a publication of the Protein Society · 2022Article
- The Mechanism of Energy Coupling in HInternational journal of molecular sciences · 2022Review
- Sucrose nonfermenting-1-related protein kinase 1 regulates sheath-to-panicle transport of nonstructural carbohydrates during rice grain filling.Plant physiology · 2022Article
- Transport efficiency of AtGTR1 dependents on the hydrophobicity of transported glucosinolates.Scientific reports · 2022Article
15 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
H(+)-translocating pyrophosphatases (H(+)-PPases) are active proton transporters that establish a proton gradient across the endomembrane by means of pyrophosphate (PP(i)) hydrolysis. H(+)-PPases are found primarily as homodimers in the vacuolar membrane of plants and the plasma membrane of several protozoa and prokaryotes. The three-dimensional structure and detailed mechanisms underlying the enzymatic and proton translocation reactions of H(+)-PPases are unclear. Here we report the crystal structure of a Vigna radiata H(+)-PPase (VrH(+)-PPase) in complex with a non-hydrolysable substrate analogue, imidodiphosphate (IDP), at 2.35 Å resolution. Each VrH(+)-PPase subunit consists of an integral membrane domain formed by 16 transmembrane helices. IDP is bound in the cytosolic region of each subunit and trapped by numerous charged residues and five Mg(2+) ions. A previously undescribed proton translocation pathway is formed by six core transmembrane helices. Proton pumping can be initialized by PP(i) hydrolysis, and H(+) is then transported into the vacuolar lumen through a pathway consisting of Arg 242, Asp 294, Lys 742 and Glu 301. We propose a working model of the mechanism for the coupling between proton pumping and PP(i) hydrolysis by H(+)-PPases.
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Registered trials
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.