ArticleJournal of bacteriology2008
The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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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.
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Who cites it
17 citing papers in PubMed, 48 citations in OpenAlex.
- Limits of a Glycine Betaine-Derived Xenobiotic as a Trojan Horse Antimicrobial.International journal of molecular sciences · 2026Article
- Structure and mechanism of the osmoregulated choline transporter BetT.Science advances · 2024Article
- Transcriptomics ofFrontiers in bioengineering and biotechnology · 2023Article
- Investigations of Dimethylglycine, Glycine Betaine, and Ectoine Uptake by a Betaine-Carnitine-Choline Transporter Family Transporter with Diverse Substrate Specificity inJournal of bacteriology · 2020Article
- Transcriptome Analysis of Gene Expression inMicroorganisms · 2020Article
- 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
- Dimethylglycine provides salt and temperature stress protection to Bacillus subtilis.Applied and environmental microbiology · 2014Article
- Osmotic control of opuA expression in Bacillus subtilis and its modulation in response to intracellular glycine betaine and proline pools.Journal of bacteriology · 2013Article
- Identification of a third osmoprotectant transport system, the osmU system, in Salmonella enterica.Journal of bacteriology · 2012Article
- Genetic control of osmoadaptive glycine betaine synthesis in Bacillus subtilis through the choline-sensing and glycine betaine-responsive GbsR repressor.Journal of bacteriology · 2012Article
- Proline utilization by Bacillus subtilis: uptake and catabolism.Journal of bacteriology · 2012Article
- Ligand binding and crystal structures of the substrate-binding domain of the ABC transporter OpuA.PloS one · 2010Article
- The ATP-binding cassette transporter Cbc (choline/betaine/carnitine) recruits multiple substrate-binding proteins with strong specificity for distinct quaternary ammonium compounds.Molecular microbiology · 2010Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the soil bacterium Bacillus subtilis, five transport systems work in concert to mediate the import of various compatible solutes that counteract the deleterious effects of increases in the osmolarity of the environment. Among these five systems, the ABC transporter OpuA, which catalyzes the import of glycine betaine and proline betaine, has been studied in detail in the past. Here, we demonstrate that OpuA is capable of importing the sulfobetaine dimethylsulfonioacetate (DMSA). Since OpuA is a classic ABC importer that relies on a substrate-binding protein priming the transporter with specificity and selectivity, we analyzed the OpuA-binding protein OpuAC by structural and mutational means with respect to DMSA binding. The determined crystal structure of OpuAC in complex with DMSA at a 2.8-A resolution and a detailed mutational analysis of these residues revealed a hierarchy within the amino acids participating in substrate binding. This finding is different from those for other binding proteins that recognize compatible solutes. Furthermore, important principles that enable OpuAC to specifically bind various compatible solutes were uncovered.
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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.