The HPr Proteins from the Thermophile Bacillus stearothermophilus can form Domain-swapped Dimers

Sridharan, Sridha; Razvi, Abbas; Scholtz, J. Martin; Sacchettini, James C.

doi:10.1016/j.jmb.2004.12.008

Cited by 16 publications

(28 citation statements)

References 49 publications

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“…Also, EIIA Ntr , a protein homologous to EIIAs that are functional in sugar transport, crystallizes as a dimer (73), although it seems to be a monomer in solution (927). Crh, an HPr-like protein of B. subtilis, was shown to form homodimers in crystals (644), and F29W HPr from Geobacillus stearothermophilus (previously Bacillus stearothermophilus) forms similar domain-swapped dimers in crystallization experiments (827). On the other hand, several measurements performed with the protein in solution suggested that F29W HPr forms monomers.…”

Section: The Phosphoenolpyruvate:carbohydrate Phosphotransferase Systemmentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,204

769

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SUMMARY The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.

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Section: The Phosphoenolpyruvate:carbohydrate Phosphotransferase Systemmentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,204

769

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“…Interestingly enough, these were the two regions shown to form the different domain-swapped domains in B. stearothermophilus HPr and Chr [49], [50]. However, it is important to indicate that, at this stage, we do not have any evidence of domain-swapping in the high-molecular-weight species of HPr bs .…”

Section: Discussionmentioning

confidence: 79%

“…A mutant of B. stearothermophilus HPr (at the Phe29 position, in the in-between loop of the first α-helix and the second β-strand) showed the presence of domain-swapped dimers in X-ray structures; this dimer, however, was not detected in solution by any hydrodynamic technique [49] (probably, because the concentrations used in the hydrodynamic measurements were not as high as those used during crystallization). The structure of the swapped-domain involves swapping of residues 56–88, the C-terminal β-strand and α-helix of one monomer, for the corresponding elements in the other monomer.…”

Section: Discussionmentioning

confidence: 99%

The Histidine-Phosphocarrier Protein of the Phosphoenolpyruvate: Sugar Phosphotransferase System of Bacillus sphaericus Self-Associates

et al. 2013

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The phosphotransferase system (PTS) is involved in the use of carbon sources in bacteria. Bacillus sphaericus, a bacterium with the ability to produce insecticidal proteins, is unable to use hexoses and pentoses as the sole carbon source, but it has ptsHI genes encoding the two general proteins of the PTS: enzyme I (EI) and the histidine phosphocarrier (HPr). In this work, we describe the biophysical and structural properties of HPr from B. sphaericus, HPrbs, and its affinity towards EI of other species to find out whether there is inter-species binding. Conversely to what happens to other members of the HPr family, HPrbs forms several self-associated species. The conformational stability of the protein is low, and it unfolds irreversibly during heating. The protein binds to the N-terminal domain of EI from Streptomyces coelicolor, EINsc, with a higher affinity than that of the natural partner of EINsc, HPrsc. Modelling of the complex between EINsc and HPrbs suggests that binding occurs similarly to that observed in other HPr species. We discuss the functional implications of the oligomeric states of HPrbs for the glycolytic activity of B. sphaericus, as well as a strategy to inhibit binding between HPrsc and EINsc.

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“…7 HPr is known to be a monomer. A recent publication 19 showed nevertheless that variants of HPr from Bacillus stearothermophilus could also form dimers via domain swapping. Interestingly, the structure of the domain-swapped dimer of HPr is very different from that observed with Crh.…”

Section: Domain-swapped Dimermentioning

confidence: 99%

X‐ray structure of a domain‐swapped dimer of Ser46‐phosphorylated Crh from Bacillus subtilis

Chaptal¹,

Larivière²,

Gueguen-Chaignon³

et al. 2006

Proteins

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The HPr Proteins from the Thermophile Bacillus stearothermophilus can form Domain-swapped Dimers

Cited by 16 publications

References 49 publications

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

The Histidine-Phosphocarrier Protein of the Phosphoenolpyruvate: Sugar Phosphotransferase System of Bacillus sphaericus Self-Associates

X‐ray structure of a domain‐swapped dimer of Ser46‐phosphorylated Crh from Bacillus subtilis

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