Domain dislocation: a change of core structure in periplasmic binding proteins in their evolutionary history

Fukami-Kobayashi, Kaoru; Tateno, Yoshio; Nishikawa, Ken

doi:10.1006/jmbi.1998.2454

Cited by 202 publications

(220 citation statements)

References 48 publications

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“…PrgZ* Complexed with cCF10-Based on the connectivity of the ␤-strands, PrgZ* has the typical type II fold of substrate-binding proteins, with two ␣/␤-domains that enclose the bound ligand (28). PrgZ has an extra domain, as has been previously described for OppA from S. typhimurium and L. lactis (14,29), and thus has a total of three domains (domains I-III).…”

Section: Resultsmentioning

confidence: 94%

Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ

Berntsson

Schuurman-Wolters

Dunny

et al. 2012

Journal of Biological Chemistry

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Background: A sex pheromone system controls bacterial conjugation. Results: The initial receptor PrgZ has been crystallized in complex with the sex pheromone cCF10. Conclusion: An extensive network of hydrogen bonds explains the high peptide specificity of PrgZ. Significance: The sex pheromone and inhibitor peptide compete for binding to PrgZ, providing new insight into the regulation of conjugation.

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Section: Resultsmentioning

confidence: 94%

Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ

Berntsson

Schuurman-Wolters

Dunny

et al. 2012

Journal of Biological Chemistry

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“…PBPs form a large protein family [4], among which glucose/galactose-binding protein binds glucose and galactose with high affinity. This construct undergoes a decrease in FRET upon substrate binding and has been used successfully to estimate changes in intracellular sugar concentration.…”

Section: Introductionmentioning

confidence: 99%

Dynamic modulation of intracellular glucose imaged in single cells using a FRET-based glucose nanosensor

John

Ottolia

Weiss

et al. 2007

Pflugers Arch - Eur J Physiol

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To study intracellular glucose homeostasis, the glucose nanosensor FLIPglu-600µM, which undergoes changes in fluorescence resonance energy transfer (FRET) upon interaction with glucose, was expressed in four mammalian cell lines: COS-7, CHO, HEK293, and C2C12. Upon addition of extracellular glucose, the intracellular FRET ratio decreased rapidly as intracellular glucose increased. The kinetics were fast (τ =5 to 15 s) in COS and C2C12 cells and slow (τ =20 to 40 s) in HEK and CHO cells. Upon removal of extracellular glucose, the FRET ratio returned to © Springer-Verlag 2007 Correspondence to: Bernard Ribalet, bribalet@mednet.ucla.edu. its initial value at similar rates (τ = 15 to 40 s) in all cell types. In all cell types, the glucose uptake FRET signal was blocked by the glucose transporter (GLUTx) inhibitor cytochalasin B and was not affected by the Na/glucose transporter inhibitor phlorizin. Glucose clearance was inhibited by the glycolytic inhibitor iodoacetate. Using β-escin to permeabilize the cell, we found that the glucose gradient across the membrane was strongly dependent on the rates of glucose uptake versus glucose clearance. With 10 mM extracellular glucose and a high rate of glucose clearance, intracellular glucose level fell below 100 µM when glucose uptake rate was low, whereas it exceeded 0.5 mM when glucose uptake was high. Cells cultured in high glucose maintained lower basal intracellular glucose levels than cells cultured in low glucose, attributed to "reciprocal regulation" of glycolysis and gluconeogenesis. Basal glucose level also increased with elevated temperatures. Experiments performed with C2C12 cells demonstrated a shift from fast glucose uptake to slow glucose uptake in the absence of insulin during differentiation. NIH Public Access

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“…Until 1998, all of the known PBP structures could be classified into two groups depending on the topology of the connection between the two lobes (23). The crystal structures of two metal binding proteins in the solute-binding protein family, however, show a very different connection between the two domains, forming a new family of metal binding receptors (24).…”

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confidence: 99%

Crystal Structures of the Liganded and Unliganded Nickel-binding Protein NikA from Escherichia coli

Heddle

Scott

Unzai

et al. 2003

Journal of Biological Chemistry

114

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Bacteria have evolved a number of tightly controlled import and export systems to maintain intracellular levels of the essential but potentially toxic metal nickel. Nickel homeostasis systems include the dedicated nickel uptake system nik found in Escherichia coli, a member of the ABC family of transporters, that involves a periplasmic nickel-binding protein, NikA. This is the initial nickel receptor and mediator of the chemotactic response away from nickel. We have solved the crystal structure of NikA protein in the presence and absence of nickel, showing that it behaves as a "classical" periplasmic binding protein. In contrast to other binding proteins, however, the ligand remains accessible to the solvent and is not completely enclosed. No direct bonds are formed between the metal cation and the protein. The nickel binding site is apolar, quite unlike any previously characterized protein nickel binding site. Despite relatively weak binding, NikA is specific for nickel. Using isothermal titration calorimetry, the dissociation constant for nickel was found to be ϳ10 M and that for cobalt was approximately 20 times higher.

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Domain dislocation: a change of core structure in periplasmic binding proteins in their evolutionary history

Cited by 202 publications

References 48 publications

Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ

Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ

Dynamic modulation of intracellular glucose imaged in single cells using a FRET-based glucose nanosensor

Crystal Structures of the Liganded and Unliganded Nickel-binding Protein NikA from Escherichia coli

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