HPr Kinase/Phosphorylase, the Sensor Enzyme of Catabolite Repression in Gram-Positive Bacteria: Structural Aspects of the Enzyme and the Complex with Its Protein Substrate
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[1] J. Walker,et al. Distantly related sequences in the alpha‐ and beta‐subunits of ATP synthase, myosin, kinases and other ATP‐requiring enzymes and a common nucleotide binding fold. , 1982, The EMBO journal.
[2] M. Saier,et al. ATP-dependent protein kinase-catalyzed phosphorylation of a seryl residue in HPr, a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes. , 1983, Proceedings of the National Academy of Sciences of the United States of America.
[3] P. Postma,et al. Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria. , 1985, Microbiological reviews.
[4] J. Deutscher,et al. Streptococcal phosphoenolpyruvate: sugar phosphotransferase system: purification and characterization of a phosphoprotein phosphatase which hydrolyzes the phosphoryl bond in seryl-phosphorylated histidine-containing protein , 1985, Journal of bacteriology.
[5] K. Beyreuther,et al. Streptococcal phosphoenolpyruvate-sugar phosphotransferase system: amino acid sequence and site of ATP-dependent phosphorylation of HPr. , 1986, Biochemistry.
[6] M. Wittekind,et al. Common structural changes accompany the functional inactivation of HPr by seryl phosphorylation or by serine to aspartate substitution. , 1989, Biochemistry.
[7] P. R. Sibbald,et al. The P-loop--a common motif in ATP- and GTP-binding proteins. , 1990, Trends in biochemical sciences.
[8] W. Nicholson,et al. Catabolite repression of α amylase gene expression in Bacillus subtilis involves a trans‐acting gene product homologous to the Escherichia coli lacl and galR repressors , 1991, Molecular microbiology.
[9] G R Jacobson,et al. Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. , 1993, Microbiological reviews.
[10] D. Liao,et al. Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins. , 1994, Structure.
[11] A G Murzin,et al. SCOP: a structural classification of proteins database for the investigation of sequences and structures. , 1995, Journal of molecular biology.
[12] Y. Fujita,et al. Specific recognition of the Bacillus subtilis gnt cis‐acting catabolite‐responsive element by a protein complex formed between CcpA and seryl‐phosphorylated HPr , 1995, Molecular microbiology.
[13] W. Hillen,et al. Protein kinase‐dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram‐positive bacteria , 1995, Molecular microbiology.
[14] L. Delbaere,et al. Snapshot of an enzyme reaction intermediate in the structure of the ATP–Mg2+–oxalate ternary complex of Escherichia coli PEP carboxykinase , 1996, Nature Structural Biology.
[15] Pyrophosphate is a source of phosphoryl groups for Escherichia coli protein phosphorylation. , 1996, FEMS microbiology letters.
[16] L. Delbaere,et al. Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold. , 1996, Journal of molecular biology.
[17] R. Klevit,et al. Binding of the Catabolite Repressor Protein CcpA to Its DNA Target Is Regulated by Phosphorylation of its Corepressor HPr* , 1997, The Journal of Biological Chemistry.
[18] L. Delbaere,et al. Mg2+–Mn2+ clusters in enzyme-catalyzed phosphoryl-transfer reactions , 1997, Nature Structural Biology.
[19] C Vonrhein,et al. The structure of a trimeric archaeal adenylate kinase. , 1998, Journal of molecular biology.
[20] O. Herzberg,et al. Topography of the interaction of HPr(Ser) kinase with HPr. , 1998, Biochemistry.
[21] J. Deutscher,et al. New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[22] C. Rivolta,et al. A novel protein kinase that controls carbon catabolite repression in bacteria , 1998, Molecular microbiology.
[23] J. Deutscher,et al. The hprK gene of Enterococcus faecalis encodes a novel bifunctional enzyme: the HPr kinase/phosphatase , 1999, Molecular microbiology.
[24] L. Delbaere,et al. The 1.9 A resolution structure of phospho-serine 46 HPr from Enterococcus faecalis. , 2000, Journal of molecular biology.
[25] A. Ogiwara,et al. Evaluation and characterization of catabolite-responsive elements (cre) of Bacillus subtilis. , 2000, Nucleic acids research.
[26] A. di Pietro,et al. The HPr Kinase from Bacillus subtilis Is a Homo-oligomeric Enzyme Which Exhibits Strong Positive Cooperativity for Nucleotide and Fructose 1,6-Bisphosphate Binding* , 2000, The Journal of Biological Chemistry.
[27] V. Monedero,et al. Phosphorylation of HPr by the Bifunctional HPr Kinase/P-Ser-HPr Phosphatase from Lactobacillus casei Controls Catabolite Repression and Inducer Exclusion but Not Inducer Expulsion , 2000, Journal of bacteriology.
[28] International Human Genome Sequencing Consortium. Initial sequencing and analysis of the human genome , 2001, Nature.
[29] L. Prasad,et al. The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3). , 2001, Journal of molecular biology.
[30] J. Janin,et al. X‐ray structure of HPr kinase: a bacterial protein kinase with a P‐loop nucleotide‐binding domain , 2001, The EMBO journal.
[31] O. Kuipers,et al. Regulatory Functions of Serine-46-Phosphorylated HPr in Lactococcus lactis , 2001, Journal of bacteriology.
[32] R. Losick,et al. Bacillus Subtilis and Its Closest Relatives: From Genes to Cells , 2001 .
[33] O. Dideberg,et al. Crystal Structure of UDP-N-acetylmuramoyl-l-alanyl-d-glutamate:meso-Diaminopimelate Ligase from Escherichia Coli * , 2001, The Journal of Biological Chemistry.
[34] W. Weyler,et al. Catabolite repression mediated by the CcpA protein in Bacillus subtilis: novel modes of regulation revealed by whole‐genome analyses , 2001, Molecular microbiology.
[35] J. V. Moran,et al. Initial sequencing and analysis of the human genome. , 2001, Nature.
[36] V. Monedero,et al. Mutations lowering the phosphatase activity of HPr kinase/phosphatase switch off carbon metabolism , 2001, The EMBO journal.
[37] Wolfgang Hengstenberg,et al. Evolutionary relationship between the bacterial HPr kinase and the ubiquitous PEP‐carboxykinase: expanding the P‐loop nucleotidyl transferase superfamily , 2002, FEBS letters.
[38] Kuang-Yu Hu,et al. Phylogeny of phosphoryl transfer proteins of the phosphoenolpyruvate-dependent sugar-transporting phosphotransferase system. , 2002, Research in microbiology.
[39] J. Janin,et al. Structural basis of macromolecular recognition. , 2002, Advances in protein chemistry.
[40] Christophe Geourjon,et al. A New Family of Phosphotransferases with a P-loop Motif* , 2002, The Journal of Biological Chemistry.
[41] W. Hillen,et al. HPr kinase/phosphatase of Bacillus subtilis: expression of the gene and effects of mutations on enzyme activity, growth and carbon catabolite repression. , 2002, Microbiology.
[42] Joël Janin,et al. Welcome to CAPRI: A Critical Assessment of PRedicted Interactions , 2002 .
[43] Jean-Michel Jault,et al. Insights into the functioning of Bacillus subtilis HPr kinase/phosphatase: affinity for its protein substrates and role of cations and phosphate. , 2002, Biochemistry.
[44] Ruth Nussinov,et al. Principles of docking: An overview of search algorithms and a guide to scoring functions , 2002, Proteins.
[45] A. Valencia,et al. Computational methods for the prediction of protein interactions. , 2002, Current opinion in structural biology.
[46] Ivan Mijakovic,et al. Pyrophosphate-producing protein dephosphorylation by HPr kinase/phosphorylase: A relic of early life? , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[47] Wolfgang Hengstenberg,et al. Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 Å resolution: Mimicking the product/substrate of the phospho transfer reactions , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[48] Ivan Mijakovic,et al. X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[49] W. Hillen,et al. A novel mode of control of Mycoplasma pneumoniae HPr kinase/phosphatase activity reflects its parasitic lifestyle. , 2002, Microbiology.
[50] Isabelle Martin-Verstraete,et al. Carbohydrate Uptake and Metabolism , 2002 .
[51] J. Deutscher,et al. Transcription Regulators Potentially Controlled by HPr Kinase/Phosphorylase in Gram-Negative Bacteria , 2003, Journal of Molecular Microbiology and Biotechnology.
[52] Sandor Vajda,et al. CAPRI: A Critical Assessment of PRedicted Interactions , 2003, Proteins.
[53] Ruth Nussinov,et al. Taking geometry to its edge: Fast unbound rigid (and hinge‐bent) docking , 2003, Proteins.
[54] R. Abagyan,et al. ICM‐DISCO docking by global energy optimization with fully flexible side‐chains , 2003, Proteins.
[55] S. Wodak,et al. Assessment of blind predictions of protein–protein interactions: Current status of docking methods , 2003, Proteins.
[56] Z. Weng,et al. ZDOCK predictions for the CAPRI challenge , 2003, Proteins.
[57] Jacques Haiech,et al. Properties and Regulation of the Bifunctional Enzyme HPr Kinase/Phosphatase in Bacillus subtilis * , 2003, The Journal of Biological Chemistry.
[58] R. Brennan,et al. Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae. , 2003, Journal of molecular biology.
[59] Efrat Ben-Zeev,et al. Prediction of the unknown: Inspiring experience with the CAPRI experiment , 2003, Proteins.