ArticleNature2014
Visualizing the kinetic power stroke that drives proton-coupled zinc(II) transport.
Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
59 citing papers in PubMed.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- In-Cell Fast Photochemical Oxidation Interrogates the Native Structure of Integral Membrane Proteins.Angewandte Chemie (International ed. in English) · 2025Article
- Enabling simultaneous photoluminescence spectroscopy and X-ray footprinting mass spectrometry to study protein conformation and interactions.Analytical methods : advancing methods and applications · 2025Article
- Cryo-EM structures of the zinc transporters ZnT3 and ZnT4 provide insights into their transport mechanisms.FEBS letters · 2025Article
- Structural insights into human zinc transporter ZnT1 mediated ZnEMBO reports · 2024Article
- Structural insights into the calcium-coupled zinc export of human ZnT1.Science advances · 2024Article
- Structures, Mechanisms, and Physiological Functions of Zinc Transporters in Different Biological Kingdoms.International journal of molecular sciences · 2024Review
- Metalation and activation of ZnBiophysics reviews · 2023Review
- A Novel Platform for Evaluating Dose Rate Effects on Oxidative Damage to Peptides: Toward a High-Throughput Method to Characterize the Mechanisms Underlying the FLASH Effect.Radiation research · 2023Article
- Energy coupling and stoichiometry of ZneLife · 2023Article
- Somatic SLC30A1 mutations altering zinc transporter ZnT1 cause aldosterone-producing adenomas and primary aldosteronism.Nature genetics · 2023Article
- Intact mass spectrometry screening to optimize hydroxyl radical dose for protein footprinting.Biochemical and biophysical research communications · 2023Article
- An automated liquid jet for fluorescence dosimetry and microsecond radiolytic labeling of proteins.Communications biology · 2022Article
- Mechanism of Zinc Transport through the Zinc Transporter YiiP.Journal of chemical theory and computation · 2022Article
- Review
- MEMBRANE PROTEIN STRUCTURES AND INTERACTIONS FROM COVALENT LABELING COUPLED WITH MASS SPECTROMETRY.Mass spectrometry reviews · 2022Review
- Iron Homeostasis in Pseudomonas aeruginosa: Targeting Iron Acquisition and Storage as an Antimicrobial Strategy.Advances in experimental medicine and biology · 2022Article
- The Oxidative Balance Orchestrates the Main Keystones of the Functional Activity of Cardiomyocytes.Oxidative medicine and cellular longevity · 2022Review
- Nanoparticles and photochemistry for native-like transmembrane protein footprinting.Nature communications · 2021Article
- New high-throughput endstation to accelerate the experimental optimization pipeline for synchrotron X-ray footprinting.Journal of synchrotron radiation · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
The proton gradient is a principal energy source for respiration-dependent active transport, but the structural mechanisms of proton-coupled transport processes are poorly understood. YiiP is a proton-coupled zinc transporter found in the cytoplasmic membrane of Escherichia coli. Its transport site receives protons from water molecules that gain access to its hydrophobic environment and transduces the energy of an inward proton gradient to drive Zn(II) efflux. This membrane protein is a well-characterized member of the family of cation diffusion facilitators that occurs at all phylogenetic levels. Here we show, using X-ray-mediated hydroxyl radical labelling of YiiP and mass spectrometry, that Zn(II) binding triggers a highly localized, all-or-nothing change of water accessibility to the transport site and an adjacent hydrophobic gate. Millisecond time-resolved dynamics reveal a concerted and reciprocal pattern of accessibility changes along a transmembrane helix, suggesting a rigid-body helical re-orientation linked to Zn(II) binding that triggers the closing of the hydrophobic gate. The gated water access to the transport site enables a stationary proton gradient to facilitate the conversion of zinc-binding energy to the kinetic power stroke of a vectorial zinc transport. The kinetic details provide energetic insights into a proton-coupled active-transport reaction.
Indexed as
Identifiers
What OpenQuestion holds
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.