ArticlePloS one2010
Ligand binding and crystal structures of the substrate-binding domain of the ABC transporter OpuA.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 49 citations in OpenAlex.
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- How arginine inhibits substrate-binding domain 2 elucidated using molecular dynamics simulations.Protein science : a publication of the Protein Society · 2024Article
- Ubiquitous occurrence of a dimethylsulfoniopropionate ABC transporter in abundant marine bacteria.The ISME journal · 2023Article
- Discovery and structure of a widespread bacterial ABC transporter specific for ergothioneine.Nature communications · 2022Article
- ProX from marine Synechococcus spp. show a sole preference for glycine-betaine with differential affinity between ecotypes.Environmental microbiology · 2022Article
- Structural insights into choline-O-sulfatase reveal the molecular determinants for ligand binding.Acta crystallographica. Section D, Structural biology · 2022Article
- Review
- Structural dynamics in the evolution of a bilobed protein scaffold.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- In silico method for selecting residue pairs for single-molecule microscopy and spectroscopy.Scientific reports · 2021Article
- Gating by ionic strength and safety check by cyclic-di-AMP in the ABC transporter OpuA.Science advances · 2020Article
- Substrate recognition and ATPase activity of theThe Journal of biological chemistry · 2020Article
- Determining the pharmacokinetics of nicotinic drugs in the endoplasmic reticulum using biosensors.The Journal of general physiology · 2019Article
- Article
- Examination of the Glycine Betaine-Dependent Methylotrophic Methanogenesis Pathway: Insights Into Anaerobic Quaternary Amine Methylotrophy.Frontiers in microbiology · 2019Article
- OpuF, a New Bacillus Compatible Solute ABC Transporter with a Substrate-Binding Protein Fused to the Transmembrane Domain.Applied and environmental microbiology · 2018Article
- Structural and Mechanistic Analysis of the Choline Sulfatase from Sinorhizobium melliloti: A Class I Sulfatase Specific for an Alkyl Sulfate Ester.Journal of molecular biology · 2018Article
- The GbsR Family of Transcriptional Regulators: Functional Characterization of the OpuAR Repressor.Frontiers in microbiology · 2018Article
- Compatible Solute Synthesis and Import by the Moderate HalophileFrontiers in microbiology · 2018Article
- Conserved ABC Transport System Regulated by the General Stress Response Pathways of Alpha- and Gammaproteobacteria.Journal of bacteriology · 2017Article
- Mechanistic Insight into Trimethylamine N-Oxide Recognition by the Marine Bacterium Ruegeria pomeroyi DSS-3.Journal of bacteriology · 2015Article
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7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe ABC transporter OpuA from Lactococcus lactis transports glycine betaine upon activation by threshold values of ionic strength. In this study, the ligand binding characteristics of purified OpuA in a detergent-solubilized state and of its substrate-binding domain produced as soluble protein (OpuAC) was characterized. PRINCIPAL
findingsThe binding of glycine betaine to purified OpuA and OpuAC (K(D) = 4-6 microM) did not show any salt dependence or cooperative effects, in contrast to the transport activity. OpuAC is highly specific for glycine betaine and the related proline betaine. Other compatible solutes like proline and carnitine bound with affinities that were 3 to 4 orders of magnitude lower. The low affinity substrates were not noticeably transported by membrane-reconstituted OpuA. OpuAC was crystallized in an open (1.9 A) and closed-liganded (2.3 A) conformation. The binding pocket is formed by three tryptophans (Trp-prism) coordinating the quaternary ammonium group of glycine betaine in the closed-liganded structure. Even though the binding site of OpuAC is identical to that of its B. subtilis homolog, the affinity for glycine betaine is 4-fold higher.
conclusionsIonic strength did not affect substrate binding to OpuA, indicating that regulation of transport is not at the level of substrate binding, but rather at the level of translocation. The overlap between the crystal structures of OpuAC from L.lactis and B.subtilis, comprising the classical Trp-prism, show that the differences observed in the binding affinities originate from outside of the ligand binding site.
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