ArticleProtein science : a publication of the Protein Society2017
Structure of the SLC4 transporter Bor1p in an inward-facing conformation.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 45 citations in OpenAlex.
- Transport mechanism of the SLC4 proteins-Lessons from recent structural and computational studies.The Journal of biological chemistry · 2026Review
- Genome-wide identification of boron transporters (GhBORs) in upland cotton and the role of GhBOR1 in promoting flowering.BMC plant biology · 2025Article
- Molecular insights into the elevator-type mechanism of the cyanobacterial bicarbonate transporter BicA.Biophysical journal · 2025Article
- The Bor1 elevator transport cycle is subject to autoinhibition and activation.Nature communications · 2024Article
- Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA.Nature communications · 2024Article
- Cryo-EM structures of the human band 3 transporter indicate a transport mechanism involving the coupled movement of chloride and bicarbonate ions.PLoS biology · 2024Article
- Mechanism of anion exchange and small-molecule inhibition of pendrin.Nature communications · 2024Article
- Borate Transporters and SLC4 Bicarbonate Transporters Share Key Functional Properties.Membranes · 2023Article
- CryoEM structures of anion exchanger 1 capture multiple states of inward- and outward-facing conformations.Communications biology · 2022Article
- Yeast as a tool for membrane protein production and structure determination.FEMS yeast research · 2022Article
- Organization and Dynamics of the Red Blood Cell Band 3 Anion Exchanger SLC4A1: Insights From Molecular Dynamics Simulations.Frontiers in physiology · 2022Review
- Cell physiology and molecular mechanism of anion transport by erythrocyte band 3/AE1.American journal of physiology. Cell physiology · 2021Review
- The Bicarbonate Transporter (MoAE4) Localized on Both Cytomembrane and Tonoplast Promotes Pathogenesis inJournal of fungi (Basel, Switzerland) · 2021Article
- Structural and functional insights into the mechanism of action of plant borate transporters.Scientific reports · 2021Article
- Transport-coupled ubiquitination of the borate transporter BOR1 for its boron-dependent degradation.The Plant cell · 2021Article
- Helical Membrane Protein Crystallization in the New Era of Electron Cryo-Microscopy.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
- Elevator-type mechanisms of membrane transport.Biochemical Society transactions · 2020Review
- Structural insights into the gating mechanism of human SLC26A9 mediated by its C-terminal sequence.Cell discovery · 2020Article
- In silico characterization of residues essential for substrate binding of human cystine transporter, xCT.Journal of molecular modeling · 2019Article
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Bor1p is a secondary transporter in yeast that is responsible for boron transport. Bor1p belongs to the SLC4 family which controls bicarbonate exchange and pH regulation in animals as well as borate uptake in plants. The SLC4 family is more distantly related to members of the Amino acid-Polyamine-organoCation (APC) superfamily, which includes well studied transporters such as LeuT, Mhp1, AdiC, vSGLT, UraA, SLC26Dg. Their mechanism generally involves relative movements of two domains: a core domain that binds substrate and a gate domain that in many cases mediates dimerization. To shed light on conformational changes governing transport by the SLC4 family, we grew helical membrane crystals of Bor1p from Saccharomyces mikatae and determined a structure at ∼6 Å resolution using cryo-electron microscopy. To evaluate the conformation of Bor1p in these crystals, a homology model was built based on the related anion exchanger from red blood cells (AE1). This homology model was fitted to the cryo-EM density map using the Molecular Dynamics (MD) Flexible Fitting method and then relaxed by all-atom MD simulation in explicit solvent and membrane. Mapping of water accessibility indicates that the resulting structure represents an inward-facing conformation. Comparisons of the resulting Bor1p model with the X-ray structure of AE1 in an outward-facing conformation, together with MD simulations of inward-facing and outward-facing Bor1p models, suggest rigid body movements of the core domain relative to the gate domain. These movements are consistent with the rocking-bundle transport mechanism described for other members of the APC superfamily.
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