ArticleNature2012
Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP.
Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 139 citations in OpenAlex.
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- They all rock: A systematic comparison of conformational movements in LeuT-fold transporters.Structure (London, England : 1993) · 2024Article
- Structure and mechanism of the osmoregulated choline transporter BetT.Science advances · 2024Article
- Structures of human SGLT in the occluded state reveal conformational changes during sugar transport.Nature communications · 2023Article
- High-resolution structures with bound MneLife · 2023Article
- Sodium/Iodide Symporter Metastable Intermediates Provide Insights into Conformational Transition between Principal Thermodynamic States.The journal of physical chemistry. B · 2023Article
- Insights into autoregulation of a membrane protein complex by its cytoplasmic domains.Biophysical journal · 2023Article
- Cryo-EM structure of the human NKCC1 transporter reveals mechanisms of ion coupling and specificity.The EMBO journal · 2022Article
- Integrated AlphaFold2 and DEER investigation of the conformational dynamics of a pH-dependent APC antiporter.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structure of cytosine transport protein CodB provides insight into nucleobase-cation symporter 1 mechanism.The EMBO journal · 2022Article
- The Tiny Companion Matters: The Important Role of Protons in Active Transports in Plants.International journal of molecular sciences · 2022Review
- General principles of secondary active transporter function.Biophysics reviews · 2022Review
- The structure of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cation-coupled chloride cotransporters: chemical insights and disease implications.Trends in chemistry · 2021Review
- Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins.Membranes · 2021Review
- The Role of the Membrane in Transporter Folding and Activity.Journal of molecular biology · 2021Review
- Molecular Mechanism of Nramp-Family Transition Metal Transport.Journal of molecular biology · 2021Review
- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
- Investigations of Dimethylglycine, Glycine Betaine, and Ectoine Uptake by a Betaine-Carnitine-Choline Transporter Family Transporter with Diverse Substrate Specificity inJournal of bacteriology · 2020Article
24 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Betaine and Na(+) symport has been extensively studied in the osmotically regulated transporter BetP from Corynebacterium glutamicum, a member of the betaine/choline/carnitine transporter family, which shares the conserved LeuT-like fold of two inverted structural repeats. BetP adjusts its transport activity by sensing the cytoplasmic K(+) concentration as a measure for hyperosmotic stress via the osmosensing carboxy-terminal domain. BetP needs to be in a trimeric state for communication between individual protomers through several intratrimeric interaction sites. Recently, crystal structures of inward-facing BetP trimers have contributed to our understanding of activity regulation on a molecular level. Here we report new crystal structures, which reveal two conformationally asymmetric BetP trimers, capturing among them three distinct transport states. We observe a total of four new conformations at once: an outward-open apo and an outward-occluded apo state, and two closed transition states--one in complex with betaine and one substrate-free. On the basis of these new structures, we identified local and global conformational changes in BetP that underlie the molecular transport mechanism, which partially resemble structural changes observed in other sodium-coupled LeuT-like fold transporters, but show differences we attribute to the osmolytic nature of betaine, the exclusive substrate specificity and the regulatory properties of BetP.
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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.