The 1·6 Å structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis

Jia, Z.; Vandonselaar, M.; Hengstenberg, Wolfgang; Quail, J. Wilson; Delbaere, L. T. J.

doi:10.1016/0022-2836(94)90062-0

Cited by 42 publications

(46 citation statements)

References 45 publications

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“…Unexpectedly, inducer exclusion in L. casei was also prevented by the ptsH(Ile47Thr) mutation, although the amount of P-Ser-HPr detected in the S. salivarius ptsH (Ile47Thr) mutant was similar to that in the parental strain (263). The hydrophobic patch on the surface of HPr, which is formed by Ile-47, Met-48, and Met-51 in gram-positive bacteria (375), is involved in the interaction of P-Ser-HPr with CcpA (381,787) and in the interaction of HPr with EI (260) and various EIIAs (139,691,949). The finding that the L. casei ptsH(Ile47Thr) mutant does not exhibit inducer exclusion suggests that this hydrophobic patch might also be important for the interaction of P-Ser-HPr with non-PTS permeases regulated by inducer exclusion.…”

Section: Is P-ser-hpr Involved In Inducer Exclusion?mentioning

confidence: 91%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,188

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: Is P-ser-hpr Involved In Inducer Exclusion?mentioning

confidence: 91%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,188

769

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“…5A). The solution structures of a number of HPr proteins originating from different species and of Crh of B. subtilis have been solved by nuclear magnetic resonance spectroscopy, and all of them show a similar overall folding (5,16,22,42). The HPr polypeptide folds as an openfaced ␤-sandwich, with three ␣-helices (a, b, and c [ Fig.…”

Section: Sequence Motifs In Hpr-like Proteinsmentioning

confidence: 99%

CcpA-Dependent Carbon Catabolite Repression in Bacteria

Warner

Lolkema

2003

Microbiol Mol Biol Rev

233

219

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Carbon catabolite repression (CCR) by transcriptional regulators follows different mechanisms in gram-positive and gram-negative bacteria. In gram-positive bacteria, CcpA-dependent CCR is mediated by phosphorylation of the phosphoenolpyruvate:sugar phosphotransferase system intermediate HPr at a serine residue at the expense of ATP. The reaction is catalyzed by HPr kinase, which is activated by glycolytic intermediates. In this review, the distribution of CcpA-dependent CCR among bacteria is investigated by searching the public databases for homologues of HPr kinase and HPr-like proteins throughout the bacterial kingdom and by analyzing their properties. Homologues of HPr kinase are commonly observed in the phylum Firmicutes but are also found in the phyla Proteobacteria, Fusobacteria, Spirochaetes, and Chlorobi, suggesting that CcpA-dependent CCR is not restricted to gram-positive bacteria. In the α and β subdivisions of the Proteobacteria, the presence of HPr kinase appears to be common, while in the γ subdivision it is more of an exception. The genes coding for the HPr kinase homologues of the Proteobacteria are in a gene cluster together with an HPr-like protein, termed XPr, suggesting a functional relationship. Moreover, the XPr proteins contain the serine phosphorylation sequence motif. Remarkably, the analysis suggests a possible relation between CcpA-dependent gene regulation and the nitrogen regulation system (Ntr) found in the γ subdivision of the Proteobacteria. The relation is suggested by the clustering of CCR and Ntr components on the genome of members of the Proteobacteria and by the close phylogenetic relationship between XPr and NPr, the HPr-like protein in the Ntr system. In bacteria in the phylum Proteobacteria that contain HPr kinase and XPr, the latter may be at the center of a complex regulatory network involving both CCR and the Ntr system

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“…In agreement with similar structural deviations of phosphorylated serine and glutamic acid, the substitution of the regulatory Ser 46 for glutamic acid in HPr (Wittekind et al, 1989), a protein component of the bacterial PEP-dependent sugar-transport system, resulted in enzyme inactivation indistinguishable from the native phosphorylation. The crystal structure of unmodified and phospho-Ser 46 would later be determined (Jia et al, 1994) (Audette et al, 2000, and an image of the electrostatic potential shows the large surface change that accompanies phosphorylation (Figure 3). This provided the first direct evidence for the structural mimicking of a phosphate group using site-directed mutagenesis.…”

Section: Natural Amino Acids As Substitutes For Modified Amino Acidsmentioning

confidence: 99%

Studying Cell Signal Transduction with Biomimetic Point Mutations

Sieracki¹,

Komarova²

2013

Genetic Manipulation of DNA and Protein - Examples From Current Research

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The 1·6 Å structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis

Cited by 42 publications

References 45 publications

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

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

CcpA-Dependent Carbon Catabolite Repression in Bacteria

Studying Cell Signal Transduction with Biomimetic Point Mutations

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