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A structural classification of substrate‐binding proteins
Substrate‐binding proteins (SBP) are associated with a wide variety of protein complexes. The proteins are part of ATP‐binding cassette transporters for substrate uptake, ion gradient drivenExpand
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Crystal structure of the Lrp‐like transcriptional regulator from the archaeon Pyrococcus furiosus
The LrpA protein from the hyperthermophilic archaeon Pyrococcus furiosus belongs to the Lrp/AsnC family of transcriptional regulatory proteins, of which the Escherichia coli leucine‐responsiveExpand
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Crystal Structures of the Choline/Acetylcholine Substrate-binding Protein ChoX from Sinorhizobium meliloti in the Liganded and Unliganded-Closed States*
The ATP-binding cassette transporter ChoVWX is one of several choline import systems operating in Sinorhizobium meliloti. Here fluorescence-based ligand binding assays were used to quantitateExpand
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The crystal structure of the substrate-binding protein OpuBC from Bacillus subtilis in complex with choline.
Bacillus subtilis can synthesize the compatible solute glycine betaine as an osmoprotectant from an exogenous supply of the precursor choline. Import of choline is mediated by two osmoticallyExpand
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An RTX transporter tethers its unfolded substrate during secretion via a unique N-terminal domain.
Type 1 secretion systems (T1SS) catalyze the one step protein transport across the membranes of Gram-negative bacteria and are composed of an outer membrane protein, a membrane fusion protein and anExpand
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The Rate of Folding Dictates Substrate Secretion by the Escherichia coli Hemolysin Type 1 Secretion System*
Secretion of the Escherichia coli toxin hemolysin A (HlyA) is catalyzed by the membrane protein complex HlyB-HlyD-TolC and requires a secretion sequence located within the last 60 amino acids ofExpand
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The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies.
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 theExpand
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Lantibiotic Immunity: Inhibition of Nisin Mediated Pore Formation by NisI
Nisin, a 3.4 kDa antimicrobial peptide produced by some Lactococcus lactis strains is the most prominent member of the lantibiotic family. Nisin can inhibit cell growth and penetrates the targetExpand
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Biochemical Properties of Ectoine Hydroxylases from Extremophiles and Their Wider Taxonomic Distribution among Microorganisms
Ectoine and hydroxyectoine are well-recognized members of the compatible solutes and are widely employed by microorganisms as osmostress protectants. The EctABC enzymes catalyze the synthesis ofExpand
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Substrate Recognition and Specificity of the NisB Protein, the Lantibiotic Dehydratase Involved in Nisin Biosynthesis*
Nisin is a posttranslationally modified antimicrobial peptide containing the cyclic thioether amino acids lanthionine and methyllanthionine. Although much is known about its antimicrobial activityExpand
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