ArticleeLife2015
Mechanism of Na(+)-dependent citrate transport from the structure of an asymmetrical CitS dimer.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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
45 citing papers in PubMed.
- CitM mediates hydroxycitrate (HCA) uptake: insights from heterologous expression in Escherichia coli, Bacillus subtilis mutant analysis and membrane topology prediction.Biotechnology letters · 2026Article
- pH-dependent activation of the NaNature communications · 2026Article
- Elevator mechanism dynamics in a sodium-coupled dicarboxylate transporter.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Elucidation of the structure and molecular mechanisms of the aspartate antiporter.Communications biology · 2025Article
- A new class of binding-protein dependent solute transporter exemplified by the TAXI-GltS system from Bordetella pertussis.Communications biology · 2025Article
- Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA.Nature communications · 2024Article
- Structural and mechanistic basis of the central energy-converting methyltransferase complex of methanogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The crossing of two unwound transmembrane regions that is the hallmark of the NhaA structural fold is critical for antiporter activity.Scientific reports · 2024Article
- On the substrate turnover rate of NBCe1 and AE1 SLC4 transporters: structure-function considerations.Frontiers in physiology · 2024Article
- Investigation of protein family relationships with deep learning.Bioinformatics advances · 2024Article
- Conservation of knotted and slipknotted topology in transmembrane transporters.Biophysical journal · 2023Article
- Structural insights into the elevator-type transport mechanism of a bacterial ZIP metal transporter.Nature communications · 2023Article
- Uptake mechanism of iron-phytosiderophore from the soil based on the structure of yellow stripe transporter.Nature communications · 2022Article
- The barley leaf rust resistance gene Rph3 encodes a predicted membrane protein and is induced upon infection by avirulent pathotypes of Puccinia hordei.Nature communications · 2022Article
- The ups and downs of elevator-type di-/tricarboxylate membrane transporters.The FEBS journal · 2022Article
- Forty years in cryoEM of membrane proteins.Microscopy (Oxford, England) · 2022Article
- High-speed atomic force microscopy reveals a three-state elevator mechanism in the citrate transporter CitS.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Thermostability-based binding assays reveal complex interplay of cation, substrate and lipid binding in the bacterial DASS transporter, VcINDY.The Biochemical journal · 2021Article
- Slipknotted and unknotted monovalent cation-proton antiporters evolved from a common ancestor.PLoS computational biology · 2021Article
- Insights into the Role of Membrane Lipids in the Structure, Function and Regulation of Integral Membrane Proteins.International journal of molecular sciences · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The common human pathogen Salmonella enterica takes up citrate as a nutrient via the sodium symporter SeCitS. Uniquely, our 2.5 Å x-ray structure of the SeCitS dimer shows three different conformations of the active protomer. One protomer is in the outside-facing state. Two are in different inside-facing states. All three states resolve the substrates in their respective binding environments. Together with comprehensive functional studies on reconstituted proteoliposomes, the structures explain the transport mechanism in detail. Our results indicate a six-step process, with a rigid-body 31° rotation of a helix bundle that translocates the bound substrates by 16 Å across the membrane. Similar transport mechanisms may apply to a wide variety of related and unrelated secondary transporters, including important drug targets.
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.