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• W2018440425 abstract "Glucose transport in Pseudomonas putida CSV86 is mediated via a periplasmic glucose-binding protein (GBP)-dependent putative glucose ABC transporter. Here we describe a homology model and functional characterization of GBP from CSV86 (ppGBP). A whole-cell [(14)C]-glucose uptake study revealed that glucose is transported by the high-affinity intracellular phosphorylative pathway. ppGBP was cloned, over-expressed in Escherichia coli and purified to apparent homogeneity. The purified ppGBPs from both E. coli and CSV86 were found to be specific for glucose. A homology model of ppGBP was constructed that resembles the class II family of periplasmic binding proteins. The model showed highest structural similarity to GBP of Thermus thermophilus (ttGBP, rmsd 0.64 Å). Structural analysis and molecular docking studies predicted W35, W36, E41, K92, K339 and H379 of ppGBP as putative glucose-binding residues. Alanine substitution of these residues resulted in significantly reduced [(14)C]-glucose binding activity. Analysis of the operonic arrangement and structural comparative studies suggested that ppGBP and ttGBP probably originated from a common ancestor. Structural adaptations that inhibit binding of di- or trisaccharides at the glucose-binding pocket of ppGBP were also identified." @default.
• W2018440425 created "2016-06-24" @default.
• W2018440425 creator A5044509938 @default.
• W2018440425 creator A5052797532 @default.
• W2018440425 creator A5062928050 @default.
• W2018440425 date "2013-12-09" @default.
• W2018440425 modified "2023-10-03" @default.
• W2018440425 title "Periplasmic glucose-binding protein from<i>Pseudomonas putida</i>CSV86 - identification of the glucose-binding pocket by homology-model-guided site-specific mutagenesis" @default.
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• W2018440425 doi "https://doi.org/10.1111/febs.12607" @default.
• W2018440425 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24206004" @default.
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