Disease relevance of c2517

• In particular, switching from glucose-rich to glucose-limited conditions results in Escherichia coli orchestrating outer membrane changes as well as the induction of a periplasmic binding protein-dependent (ABC-type) transport system [1].
• The high affinity branched-chain amino acid transport system (LIV-I) in Pseudomonas aeruginosa is composed of five components: BraC, a periplasmic binding protein for branched-chain amino acids; BraD and BraE, integral membrane proteins; BraF and BraG, putative nucleotide-binding proteins [2].
• The Yersinia enterocolitica O:8 periplasmic binding-protein-dependent transport (PBT) system for haemin was cloned and characterized [3].
• The oligopeptide permease of Salmonella typhimurium is a periplasmic binding protein-dependent transport system [4].
• Molecular characterization of a Campylobacter jejuni 29-kilodalton periplasmic binding protein [5].

High impact information on c2517

• Periplasmic binding protein-dependent transport systems, like the maltose transport system of E.coli, possess a water-soluble ligand binding protein that is essential for transport activity [6].
• The identification of a nucleotide-binding site provides strong evidence that transport by periplasmic binding protein-dependent systems is energized directly by the hydrolysis of ATP or a closely related nucleotide [7].
• Bacterial periplasmic binding protein-dependent transport systems require the function of a specific substrate-binding protein, located in the periplasm, and several membrane-bound components [7].
• FhuD is a soluble periplasmic binding protein that transports ferrichrome and other hydroxamate siderophores [8].
• These results provide convincing evidence that it is the hydrolysis of ATP that drives maltose transport, and probably also other periplasmic-binding-protein-dependent transport systems [9].

Chemical compound and disease context of c2517

• Maltose transport across the cytoplasmic membrane of Escherichia coli is catalyzed by a periplasmic binding protein-dependent transport system and energized by ATP [10].
• Chain-terminating mutants affecting a periplasmic binding protein involved in the active transport of arginine and ornithine in Escherichia coli [11].
• The active transport of glutamine by Escherichia coli occurs via a single osmotic shock-sensitive transport system which is known to be dependent upon a periplasmic binding protein specific for glutamine [12].
• Direct measurement of opp operon expression by pulse-labeling experiments demonstrated that growth of E. coli in the presence of leucine resulted in increased synthesis of the oppA-encoded periplasmic binding protein [13].
• Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli [14].

Biological context of c2517

• Taken together, these data support the notion that the nik operon encodes a typical periplasmic binding-protein-dependent transport system for nickel [15].
• Based on DNA sequence analysis, fit encodes an outer membrane protein (FitA), a periplasmic binding protein (FitE), two permease proteins (FitC and -D), an ATPase (FitB), and a hypothetical protein (FitR) [16].
• Phosphorylation of the periplasmic binding protein in two transport systems for arginine incorporation in Escherichia coli K-12 is unrelated to the function of the transport system [17].
• Site-directed mutagenesis of the gene encoding the periplasmic binding protein (hutX) and of the gene encoding the cytoplasmic ATPase (hutV) was done to study the substrate specificity of this transporter and its contribution in betaine uptake [18].
• Previously uncharacterized potential iron transport systems, including a homologue of the ferrous transporter Feo and a periplasmic binding protein-dependent ATP binding cassette (ABC) transport system, termed Fbp, were identified in the V. cholerae genome sequence [19].

Anatomical context of c2517

• Periplasmic binding protein-dependent transport systems mediate the accumulation of many diverse substrates in prokaryotic cells [20].
• Transport across the outer membrane is receptor-dependent and energy-coupled; transport across the cytoplasmic membrane seems to follow a periplasmic binding protein-dependent transport mechanism [21].
• MppA, a periplasmic binding protein essential for import of the bacterial cell wall peptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate [22].
• Previously, we found that polymers bearing multiple copies of galactose interact with the chemoreceptor Trg via the periplasmic binding protein glucose/galactose binding protein (GGBP) [23].

Associations of c2517 with chemical compounds

• Modeling of the substrate-bound state was done by comparison of this protein with another periplasmic binding protein (L-arabinose-binding protein), which possesses a similar two-lobe structure and for which the x-ray structure is known in its ligand-bound form [24].
• Together these data indicate that ferric enterobactin is transported through a typical periplasmic binding protein-dependent system [25].
• Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine [26].
• GlnBP is a periplasmic binding protein which plays an essential role in the active transport of L-glutamine through the cytoplasmic membrane [27].
• One of the proteins involved in the transport of mercuric ion is the periplasmic binding protein MerP, which can exist both as oxidized (disulfide) and as reduced (dithiol) forms [28].

Analytical, diagnostic and therapeutic context of c2517

• Sequence analysis of the modA gene (GenBank L34009) predicts that it encodes a periplasmic binding protein based on the presence of a leader-like sequence at its N terminus [29].
• Purification, crystallization and preliminary crystallographic analysis of the periplasmic binding protein ProX from Escherichia coli [30].

References