ArticleBMC structural biology2007
Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding.
Article in BMC structural biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 72 citations in OpenAlex.
- On the function of TRAP substrate-binding proteins: the isethionate-specific binding protein IseP.The Biochemical journal · 2024Article
- Structure and selectivity of a glutamate-specific TAXI TRAP binding protein from Vibrio cholerae.The Journal of general physiology · 2024Article
- Discovery of periplasmic solute binding proteins with specificity for ketone bodies: β-hydroxybutyrate binding proteins.Protein science : a publication of the Protein Society · 2024Article
- Molecular and structural basis of oligopeptide recognition by the Ami transporter system in pneumococci.PLoS pathogens · 2024Article
- The substrate-binding domains of the osmoregulatory ABC importer OpuA transiently interact.eLife · 2024Article
- Structural and biophysical analysis of aeLife · 2024Article
- The role of oligomerization in the optimization of cyclohexadienyl dehydratase conformational dynamics and catalytic activity.Protein science : a publication of the Protein Society · 2022Article
- Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter.Nature communications · 2022Article
- Selective Nutrient Transport in Bacteria: Multicomponent Transporter Systems Reign Supreme.Frontiers in molecular biosciences · 2021Review
- Reduction of Protein Bound Methionine Sulfoxide by a Periplasmic Dimethyl Sulfoxide Reductase.Antioxidants (Basel, Switzerland) · 2020Article
- Galactitol catabolism in Sinorhizobium meliloti is dependent on a chromosomally encoded sorbitol dehydrogenase and a pSymB-encoded operon necessary for tagatose catabolism.Molecular genetics and genomics : MGG · 2019Article
- Biophysical insights into a highly selective l-arginine-binding lipoprotein of a pathogenic treponeme.Protein science : a publication of the Protein Society · 2018Article
- Tripartite ATP-Independent Periplasmic (TRAP) Transporters and Tripartite Tricarboxylate Transporters (TTT): From Uptake to Pathogenicity.Frontiers in cellular and infection microbiology · 2018Review
- A novel signal transduction protein: Combination of solute binding and tandem PAS-like sensor domains in one polypeptide chain.Protein science : a publication of the Protein Society · 2017Article
- Structural characterization of the Streptococcus pneumoniae carbohydrate substrate-binding protein SP0092.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Article
- The Tp0684 (MglB-2) Lipoprotein of Treponema pallidum: A Glucose-Binding Protein with Divergent Topology.PloS one · 2016Article
- Tripartite ATP-independent Periplasmic (TRAP) Transporters Use an Arginine-mediated Selectivity Filter for High Affinity Substrate Binding.The Journal of biological chemistry · 2015Article
- Studies of conformational changes of an arginine-binding protein from Thermotoga maritima in the presence and absence of ligand via molecular dynamics simulations with the coarse-grained UNRES force field.Journal of molecular modeling · 2015Article
- The sRNA SorY confers resistance during photooxidative stress by affecting a metabolite transporter in Rhodobacter sphaeroides.RNA biology · 2015Article
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7 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundThe import of solutes into the bacterial cytoplasm involves several types of membrane transporters, which may be driven by ATP hydrolysis (ABC transporters) or by an ion or H+ electrochemical membrane potential, as in the tripartite ATP-independent periplasmic system (TRAP). In both the ABC and TRAP systems, a specific periplasmic protein from the ESR family (Extracytoplasmic Solute Receptors) is often involved for the recruitment of the solute and its presentation to the membrane complex. In Rhodobacter sphaeroides, TakP (previously named SmoM) is an ESR from a TRAP transporter and binds alpha-keto acids in vitro.
resultsWe describe the high-resolution crystal structures of TakP in its unliganded form and as a complex with sodium-pyruvate. The results show a limited "Venus flytrap" conformational change induced by substrate binding. In the liganded structure, a cation (most probably a sodium ion) is present and plays a key role in the association of the pyruvate to the protein. The structure of the binding pocket gives a rationale for the relative affinities of various ligands that were tested from a fluorescence assay. The protein appears to be dimeric in solution and in the crystals, with a helix-swapping structure largely participating in the dimer formation. A 30 A-long water channel buried at the dimer interface connects the two ligand binding cavities of the dimer.
conclusionThe concerted recruitment by TakP of the substrate group with a cation could represent a first step in the coupled transport of both partners, providing the driving force for solute import. Furthermore, the unexpected dimeric structure of TakP suggests a molecular mechanism of solute uptake by the dimeric ESR via a channel that connects the binding sites of the two monomers.
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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.