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Volumn 34, Issue 7, 2009, Pages 351-357

Emerging structural insights into bacterial tyrosine kinases

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ANTIBIOTIC AGENT; BACTERIAL ENZYME; ESCHERICHIA COLI PROTEIN; PROTEIN CAPB; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 67649948824     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2009.03.003     Document Type: Review
Times cited : (23)

References (45)
  • 1
    • 33751272653 scopus 로고    scopus 로고
    • Structural biology of protein tyrosine kinases
    • Cowan-Jacob S.W. Structural biology of protein tyrosine kinases. Cell. Mol. Life Sci. 63 (2006) 2608-2625
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 2608-2625
    • Cowan-Jacob, S.W.1
  • 2
    • 0028968949 scopus 로고
    • Tyrosine kinase inhibition: an approach to drug development
    • Levitzki A., and Gazit A. Tyrosine kinase inhibition: an approach to drug development. Science 267 (1995) 1782-1788
    • (1995) Science , vol.267 , pp. 1782-1788
    • Levitzki, A.1    Gazit, A.2
  • 3
    • 33846683630 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology
    • Grangeasse C., et al. Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology. Trends Biochem. Sci. 32 (2007) 86-94
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 86-94
    • Grangeasse, C.1
  • 4
    • 54949108269 scopus 로고    scopus 로고
    • Identification of the idiosyncratic bacterial protein-tyrosine kinase (BY-kinase) family signature
    • Jadeau F., et al. Identification of the idiosyncratic bacterial protein-tyrosine kinase (BY-kinase) family signature. Bioinformatics 24 (2008) 2427-2430
    • (2008) Bioinformatics , vol.24 , pp. 2427-2430
    • Jadeau, F.1
  • 5
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe D.D., et al. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 317 (2002) 41-72
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1
  • 6
    • 0025048136 scopus 로고
    • The P-loop - a common motif in ATP- and GTP-binding proteins
    • Saraste M., et al. The P-loop - a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15 (1990) 430-434
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1
  • 7
    • 0141574316 scopus 로고    scopus 로고
    • Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase
    • Grangeasse C., et al. Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase. J. Biol. Chem. 278 (2003) 39323-39329
    • (2003) J. Biol. Chem. , vol.278 , pp. 39323-39329
    • Grangeasse, C.1
  • 8
    • 0141625244 scopus 로고    scopus 로고
    • Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases
    • Mijakovic I., et al. Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases. EMBO J. 22 (2003) 4709-4718
    • (2003) EMBO J. , vol.22 , pp. 4709-4718
    • Mijakovic, I.1
  • 9
    • 22544486262 scopus 로고    scopus 로고
    • Identification of an Escherichia coli operon required for formation of the O-antigen capsule
    • Peleg A., et al. Identification of an Escherichia coli operon required for formation of the O-antigen capsule. J. Bacteriol. 187 (2005) 5259-5266
    • (2005) J. Bacteriol. , vol.187 , pp. 5259-5266
    • Peleg, A.1
  • 10
    • 47249110762 scopus 로고    scopus 로고
    • Transient shielding of intimin and the type III secretion system of enterohemorrhagic and enteropathogenic Escherichia coli by a group 4 capsule
    • Shifrin Y., et al. Transient shielding of intimin and the type III secretion system of enterohemorrhagic and enteropathogenic Escherichia coli by a group 4 capsule. J. Bacteriol. 190 (2008) 5063-5074
    • (2008) J. Bacteriol. , vol.190 , pp. 5063-5074
    • Shifrin, Y.1
  • 11
    • 33747299304 scopus 로고    scopus 로고
    • A novel role for protein-tyrosine kinase Etk from Escherichia coli K-12 related to polymyxin resistance
    • Lacour S., et al. A novel role for protein-tyrosine kinase Etk from Escherichia coli K-12 related to polymyxin resistance. Res. Microbiol. 157 (2006) 637-641
    • (2006) Res. Microbiol. , vol.157 , pp. 637-641
    • Lacour, S.1
  • 12
    • 47049095612 scopus 로고    scopus 로고
    • Structure of Escherichia coli tyrosine kinase Etk reveals a novel activation mechanism
    • Lee D.C., et al. Structure of Escherichia coli tyrosine kinase Etk reveals a novel activation mechanism. EMBO J. 27 (2008) 1758-1766
    • (2008) EMBO J. , vol.27 , pp. 1758-1766
    • Lee, D.C.1
  • 13
    • 0037384743 scopus 로고    scopus 로고
    • Phosphorylation-mediated regulation of heat shock response in Escherichia coli
    • Klein G., et al. Phosphorylation-mediated regulation of heat shock response in Escherichia coli. Mol. Microbiol. 48 (2003) 269-285
    • (2003) Mol. Microbiol. , vol.48 , pp. 269-285
    • Klein, G.1
  • 14
    • 33645466839 scopus 로고    scopus 로고
    • Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine
    • Mijakovic I., et al. Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine. Nucleic Acids Res. 34 (2006) 1588-1596
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1588-1596
    • Mijakovic, I.1
  • 15
    • 33847037161 scopus 로고    scopus 로고
    • Influence of tyrosine-kinase Wzc activity on colanic acid production in Escherichia coli K12 cells
    • Obadia B., et al. Influence of tyrosine-kinase Wzc activity on colanic acid production in Escherichia coli K12 cells. J. Mol. Biol. 367 (2006) 42-53
    • (2006) J. Mol. Biol. , vol.367 , pp. 42-53
    • Obadia, B.1
  • 16
    • 0036889026 scopus 로고    scopus 로고
    • Impact of phosphorylation of specific residues in the tyrosine autokinase, Wzc, on its activity in assembly of group 1 capsules in Escherichia coli
    • Paiment A., et al. Impact of phosphorylation of specific residues in the tyrosine autokinase, Wzc, on its activity in assembly of group 1 capsules in Escherichia coli. J. Bacteriol. 184 (2002) 6437-6447
    • (2002) J. Bacteriol. , vol.184 , pp. 6437-6447
    • Paiment, A.1
  • 17
    • 33746356503 scopus 로고    scopus 로고
    • Biosynthesis and assembly of capsular polysaccharides in Escherichia coli
    • Whitfield C. Biosynthesis and assembly of capsular polysaccharides in Escherichia coli. Annu. Rev. Biochem. 75 (2006) 39-68
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 39-68
    • Whitfield, C.1
  • 18
    • 45849125779 scopus 로고    scopus 로고
    • Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus
    • Olivares-Illana V., et al. Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus. PLoS Biol. 6 (2008) e143
    • (2008) PLoS Biol. , vol.6
    • Olivares-Illana, V.1
  • 19
    • 0033759266 scopus 로고    scopus 로고
    • Regulation of carbon catabolism in Bacillus species
    • Stulke J., and Hillen W. Regulation of carbon catabolism in Bacillus species. Annu. Rev. Microbiol. 54 (2000) 849-880
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 849-880
    • Stulke, J.1    Hillen, W.2
  • 20
    • 59649116252 scopus 로고    scopus 로고
    • Sequence-structure relationships in polysaccharide co-polymerase (PCP) proteins
    • Morona R., et al. Sequence-structure relationships in polysaccharide co-polymerase (PCP) proteins. Trends Biochem. Sci. 34 (2009) 78-84
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 78-84
    • Morona, R.1
  • 21
    • 38849088665 scopus 로고    scopus 로고
    • Bacterial polysaccharide co-polymerases share a common framework for control of polymer length
    • Tocilj A., et al. Bacterial polysaccharide co-polymerases share a common framework for control of polymer length. Nat. Struct. Mol. Biol. 15 (2008) 130-138
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 130-138
    • Tocilj, A.1
  • 22
    • 0037020176 scopus 로고    scopus 로고
    • Structural organization of the protein-tyrosine autokinase Wzc within Escherichia coli cells
    • Doublet P., et al. Structural organization of the protein-tyrosine autokinase Wzc within Escherichia coli cells. J. Biol. Chem. 277 (2002) 37339-37348
    • (2002) J. Biol. Chem. , vol.277 , pp. 37339-37348
    • Doublet, P.1
  • 23
    • 0036510550 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase Wzc from Escherichia coli K12 occurs through a two-step process
    • Grangeasse C., et al. Tyrosine phosphorylation of protein kinase Wzc from Escherichia coli K12 occurs through a two-step process. J. Biol. Chem. 277 (2002) 7127-7135
    • (2002) J. Biol. Chem. , vol.277 , pp. 7127-7135
    • Grangeasse, C.1
  • 24
    • 0035901493 scopus 로고    scopus 로고
    • Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus
    • Hayashi I., et al. Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus. EMBO J. 20 (2001) 1819-1828
    • (2001) EMBO J. , vol.20 , pp. 1819-1828
    • Hayashi, I.1
  • 25
    • 0033551256 scopus 로고    scopus 로고
    • Nucleophilic activation by positioning in phosphoryl transfer catalyzed by nucleoside diphosphate kinase
    • Admiraal S.J., et al. Nucleophilic activation by positioning in phosphoryl transfer catalyzed by nucleoside diphosphate kinase. Biochemistry 38 (1999) 4701-4711
    • (1999) Biochemistry , vol.38 , pp. 4701-4711
    • Admiraal, S.J.1
  • 26
    • 0034610305 scopus 로고    scopus 로고
    • Insights into nucleotide signal transduction in nitrogenase: structure of an iron protein with MgADP bound
    • Jang S.B., et al. Insights into nucleotide signal transduction in nitrogenase: structure of an iron protein with MgADP bound. Biochemistry 39 (2000) 14745-14752
    • (2000) Biochemistry , vol.39 , pp. 14745-14752
    • Jang, S.B.1
  • 27
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
    • Holland I.B., and Blight M.A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 293 (1999) 381-399
    • (1999) J. Mol. Biol. , vol.293 , pp. 381-399
    • Holland, I.B.1    Blight, M.A.2
  • 28
    • 13444281991 scopus 로고    scopus 로고
    • Bacterial chromosome segregation: structure and DNA binding of the Soj dimer - a conserved biological switch
    • Leonard T.A., et al. Bacterial chromosome segregation: structure and DNA binding of the Soj dimer - a conserved biological switch. EMBO J. 24 (2005) 270-282
    • (2005) EMBO J. , vol.24 , pp. 270-282
    • Leonard, T.A.1
  • 29
    • 0030296632 scopus 로고    scopus 로고
    • Structure and function of the protein tyrosine phosphatases
    • Fauman E.B., and Saper M.A. Structure and function of the protein tyrosine phosphatases. Trends Biochem. Sci. 21 (1996) 413-417
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 413-417
    • Fauman, E.B.1    Saper, M.A.2
  • 30
    • 34547154729 scopus 로고    scopus 로고
    • Activation segment exchange: a common mechanism of kinase autophosphorylation? Trends Biochem
    • Oliver A.W., et al. Activation segment exchange: a common mechanism of kinase autophosphorylation? Trends Biochem. Sci. 32 (2007) 351-356
    • (2007) Sci. , vol.32 , pp. 351-356
    • Oliver, A.W.1
  • 31
    • 0037133589 scopus 로고    scopus 로고
    • 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
    • Marquez J.A., 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. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 3458-3463
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 3458-3463
    • Marquez, J.A.1
  • 32
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard S.R., et al. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372 (1994) 746-754
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1
  • 33
    • 0035839434 scopus 로고    scopus 로고
    • Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation
    • Zhou T., et al. Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation. J. Biol. Chem. 276 (2001) 30414-30422
    • (2001) J. Biol. Chem. , vol.276 , pp. 30414-30422
    • Zhou, T.1
  • 34
    • 0033941641 scopus 로고    scopus 로고
    • Protein fold recognition using sequence profiles and its application in structural genomics
    • Koonin E.V., et al. Protein fold recognition using sequence profiles and its application in structural genomics. Adv. Protein Chem. 54 (2000) 245-275
    • (2000) Adv. Protein Chem. , vol.54 , pp. 245-275
    • Koonin, E.V.1
  • 35
    • 0001607723 scopus 로고
    • 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
    • Walker J.E., 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. EMBO J. 1 (1982) 945-951
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1
  • 36
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • Leipe D.D., et al. Evolution and classification of P-loop kinases and related proteins. J. Mol. Biol. 333 (2003) 781-815
    • (2003) J. Mol. Biol. , vol.333 , pp. 781-815
    • Leipe, D.D.1
  • 37
    • 0035682189 scopus 로고    scopus 로고
    • Overview: ABC transporters and human disease
    • Gottesman M.M., and Ambudkar S.V. Overview: ABC transporters and human disease. J. Bioenerg. Biomembr. 33 (2001) 453-458
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 453-458
    • Gottesman, M.M.1    Ambudkar, S.V.2
  • 38
    • 16844368698 scopus 로고    scopus 로고
    • Tumour stem cells and drug resistance
    • Dean M., et al. Tumour stem cells and drug resistance. Nat. Rev. Cancer 5 (2005) 275-284
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 275-284
    • Dean, M.1
  • 39
    • 34548853133 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporter proteins
    • Hollenstein K., et al. Structure and mechanism of ABC transporter proteins. Curr. Opin. Struct. Biol. 17 (2007) 412-418
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 412-418
    • Hollenstein, K.1
  • 40
    • 0026511990 scopus 로고
    • New minC mutations suggest different interactions of the same region of division inhibitor MinC with proteins specific for minD and dicB coinhibition pathways
    • Mulder E., et al. New minC mutations suggest different interactions of the same region of division inhibitor MinC with proteins specific for minD and dicB coinhibition pathways. J. Bacteriol. 174 (1992) 35-39
    • (1992) J. Bacteriol. , vol.174 , pp. 35-39
    • Mulder, E.1
  • 41
    • 0034120118 scopus 로고    scopus 로고
    • Control of sporulation gene expression in Bacillus subtilis by the chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
    • Quisel J.D., and Grossman A.D. Control of sporulation gene expression in Bacillus subtilis by the chromosome partitioning proteins Soj (ParA) and Spo0J (ParB). J. Bacteriol. 182 (2000) 3446-3451
    • (2000) J. Bacteriol. , vol.182 , pp. 3446-3451
    • Quisel, J.D.1    Grossman, A.D.2
  • 42
    • 0030611701 scopus 로고    scopus 로고
    • --stabilized nitrogenase complex and its implications for signal transduction
    • --stabilized nitrogenase complex and its implications for signal transduction. Nature 387 (1997) 370-376
    • (1997) Nature , vol.387 , pp. 370-376
    • Schindelin, H.1
  • 43
    • 0025333199 scopus 로고
    • The plasmid-encoded arsenical resistance pump: an anion-translocating ATPase
    • Rosen B.P. The plasmid-encoded arsenical resistance pump: an anion-translocating ATPase. Res. Microbiol. 141 (1990) 336-341
    • (1990) Res. Microbiol. , vol.141 , pp. 336-341
    • Rosen, B.P.1
  • 44
    • 16644402929 scopus 로고    scopus 로고
    • A preliminary solubility screen used to improve crystallization trials: crystallization and preliminary X-ray structure determination of Aeropyrum pernix flap endonuclease-1
    • Collins B.K., et al. A preliminary solubility screen used to improve crystallization trials: crystallization and preliminary X-ray structure determination of Aeropyrum pernix flap endonuclease-1. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 1674-1678
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1674-1678
    • Collins, B.K.1
  • 45
    • 33644848881 scopus 로고    scopus 로고
    • Periplasmic protein-protein contacts in the inner membrane protein Wzc form a tetrameric complex required for the assembly of Escherichia coli group 1 capsules
    • Collins R.F., et al. Periplasmic protein-protein contacts in the inner membrane protein Wzc form a tetrameric complex required for the assembly of Escherichia coli group 1 capsules. J. Biol. Chem. 281 (2006) 2144-2150
    • (2006) J. Biol. Chem. , vol.281 , pp. 2144-2150
    • Collins, R.F.1


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