ArticleScientific reports2014
Crystal structure of the phosphate-binding protein (PBP-1) of an ABC-type phosphate transporter from Clostridium perfringens.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- A Thr/Ser-centered phosphate-binding triad of phosphate-binding protein SphX from Synechocystis.Communications biology · 2026Article
- Genomic and Proteomic Characterization of the Deltamethrin-Degrading BacteriumMicroorganisms · 2025Article
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- Doubling the Carbonate-Binding Capacity of Nanojars by the Formation of Expanded Nanojars.Molecules (Basel, Switzerland) · 2021Article
- Molecular Mechanisms of Phosphate Sensing, Transport and Signalling in Streptomyces and Related Actinobacteria.International journal of molecular sciences · 2021Review
- Masking Phosphate with Rare-Earth Elements Enables Selective Detection of Arsenate by Dipycolylamine-ZnScientific reports · 2020Article
- Exploring the rearrangement of sensory intelligence in proteobacteria: insight of Pho regulon.World journal of microbiology & biotechnology · 2018Article
- Phosphate-binding protein from Polaromonas JS666: purification, characterization, crystallization and sulfur SAD phasing.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Paralogous Regulators ArsR1 and ArsR2 of Pseudomonas putida KT2440 as a Basis for Arsenic Biosensor Development.Applied and environmental microbiology · 2016Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Phosphate limitation is an important environmental stress that affects the metabolism of various organisms and, in particular, can trigger the virulence of numerous bacterial pathogens. Clostridium perfringens, a human pathogen, is one of the most common causes of enteritis necroticans, gas gangrene and food poisoning. Here, we focused on the high affinity phosphate-binding protein (PBP-1) of an ABC-type transporter, responsible for cellular phosphate uptake. We report the crystal structure (1.65 Å resolution) of the protein in complex with phosphate. Interestingly, PBP-1 does not form the short, low-barrier hydrogen bond with phosphate that is typical of previously characterized phosphate-binding proteins, but rather a canonical hydrogen bond. In its unique binding configuration, PBP-1 forms an unusually high number of hydrogen bonds (14) with the phosphate anion. Discrimination experiments reveal that PBP-1 is the least selective PBP characterised so far and is able to discriminate phosphate from its close competing anion, arsenate, by ~150-fold.
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