메뉴 건너뛰기




Volumn 172, Issue 3, 2010, Pages 319-330

Solution structure and phospho-PmrA recognition mode of PmrD from Klebsiella pneumoniae

Author keywords

BeF3 activation; Chemical shift perturbation; NMR; PmrD connector protein; Saturation transfer; SPR

Indexed keywords

ALANINE; ARGININE; ASPARAGINE; ASPARTIC ACID; BACTERIAL PROTEIN; BERYLLOFLUORIDE; DIMER; FLUORIDE; GLUTAMINE; HISTIDINE; ISOLEUCINE; LEUCINE; PROTEIN PMRD; SERINE; THREONINE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

EID: 77958181559     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.06.007     Document Type: Article
Times cited : (7)

References (41)
  • 1
    • 0034047384 scopus 로고    scopus 로고
    • Phosphorylated PmrA interacts with the promoter region of ugd in Salmonella enterica serovar typhimurium
    • Aguirre A., Lejona S., Vescovi E.G., Soncini F.C. Phosphorylated PmrA interacts with the promoter region of ugd in Salmonella enterica serovar typhimurium. J. Bacteriol. 2000, 182:3874-3876.
    • (2000) J. Bacteriol. , vol.182 , pp. 3874-3876
    • Aguirre, A.1    Lejona, S.2    Vescovi, E.G.3    Soncini, F.C.4
  • 2
    • 0027350599 scopus 로고
    • Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS
    • Anglister J., Grzesiek S., Ren H., Klee C.B., Bax A. Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS. J. Biomol. NMR 1993, 3:121-126.
    • (1993) J. Biomol. NMR , vol.3 , pp. 121-126
    • Anglister, J.1    Grzesiek, S.2    Ren, H.3    Klee, C.B.4    Bax, A.5
  • 3
    • 34249765651 scopus 로고
    • NMR view: a computer program for the visualization and analysis of NMR data
    • Bruce A.J., Richard A.B. NMR view: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 1994, V4:603-614.
    • (1994) J. Biomol. NMR , vol.V4 , pp. 603-614
    • Bruce, A.J.1    Richard, A.B.2
  • 5
    • 70349795241 scopus 로고    scopus 로고
    • Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
    • Casino P., Rubio V., Marina A. Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell 2009, 139:325-336.
    • (2009) Cell , vol.139 , pp. 325-336
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 6
    • 0035902464 scopus 로고    scopus 로고
    • BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase
    • Cho H., Wang W., Kim R., Yokota H., Damo S., Kim S.H., Wemmer D., Kustu S., Yan D. BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase. Proc. Natl. Acad. Sci. USA 2001, 98:8525-8530.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8525-8530
    • Cho, H.1    Wang, W.2    Kim, R.3    Yokota, H.4    Damo, S.5    Kim, S.H.6    Wemmer, D.7    Kustu, S.8    Yan, D.9
  • 10
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Gabriel C., Frank D., Ad B. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 1999, V13:289-302.
    • (1999) J. Biomol. NMR , vol.V13 , pp. 289-302
    • Gabriel, C.1    Frank, D.2    Ad, B.3
  • 12
    • 0035105303 scopus 로고    scopus 로고
    • The pleiotropic two-component regulatory system PhoP-PhoQ
    • Groisman E.A. The pleiotropic two-component regulatory system PhoP-PhoQ. J. Bacteriol. 2001, 183:1835-1842.
    • (2001) J. Bacteriol. , vol.183 , pp. 1835-1842
    • Groisman, E.A.1
  • 13
    • 0030729248 scopus 로고    scopus 로고
    • Regulation of polymyxin resistance and adaptation to low-Mg2+ environments
    • Groisman E.A., Kayser J., Soncini F.C. Regulation of polymyxin resistance and adaptation to low-Mg2+ environments. J. Bacteriol. 1997, 179:7040-7045.
    • (1997) J. Bacteriol. , vol.179 , pp. 7040-7045
    • Groisman, E.A.1    Kayser, J.2    Soncini, F.C.3
  • 15
    • 43949103402 scopus 로고    scopus 로고
    • Analysis and optimization of saturation transfer difference NMR experiments designed to map early self-association events in amyloidogenic peptides
    • Huang H., Milojevic J., Melacini G. Analysis and optimization of saturation transfer difference NMR experiments designed to map early self-association events in amyloidogenic peptides. J. Phys. Chem. B 2008, 112:5795-5802.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5795-5802
    • Huang, H.1    Milojevic, J.2    Melacini, G.3
  • 16
    • 43449100066 scopus 로고    scopus 로고
    • Allosteric and electrostatic protein-protein interactions regulate the assembly of the heterohexameric Tim9-Tim10 complex
    • Ivanova E., Lu H. Allosteric and electrostatic protein-protein interactions regulate the assembly of the heterohexameric Tim9-Tim10 complex. J. Mol. Biol. 2008, 379:609-616.
    • (2008) J. Mol. Biol. , vol.379 , pp. 609-616
    • Ivanova, E.1    Lu, H.2
  • 17
    • 4444240880 scopus 로고    scopus 로고
    • Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor
    • Kato A., Groisman E.A. Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor. Genes Dev. 2004, 18:2302-2313.
    • (2004) Genes Dev. , vol.18 , pp. 2302-2313
    • Kato, A.1    Groisman, E.A.2
  • 18
    • 34547551186 scopus 로고    scopus 로고
    • A connector of two-component regulatory systems promotes signal amplification and persistence of expression
    • Kato A., Mitrophanov A.Y., Groisman E.A. A connector of two-component regulatory systems promotes signal amplification and persistence of expression. Proc. Natl. Acad. Sci. USA 2007, 104:12063-12068.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12063-12068
    • Kato, A.1    Mitrophanov, A.Y.2    Groisman, E.A.3
  • 19
    • 0029437296 scopus 로고
    • Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution
    • Kay L.E. Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution. Prog. Biophys. Mol. Biol. 1995, 63:277-299.
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 277-299
    • Kay, L.E.1
  • 20
    • 0023715368 scopus 로고
    • Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria
    • Keen N.T., Tamaki S., Kobayashi D., Trollinger D. Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria. Gene 1988, 70:191-197.
    • (1988) Gene , vol.70 , pp. 191-197
    • Keen, N.T.1    Tamaki, S.2    Kobayashi, D.3    Trollinger, D.4
  • 21
    • 43149092276 scopus 로고    scopus 로고
    • Principles of protein-protein interactions: what are the preferred ways for proteins to interact?
    • Keskin O., Gursoy A., Ma B., Nussinov R. Principles of protein-protein interactions: what are the preferred ways for proteins to interact?. Chem. Rev. 2008, 108:1225-1244.
    • (2008) Chem. Rev. , vol.108 , pp. 1225-1244
    • Keskin, O.1    Gursoy, A.2    Ma, B.3    Nussinov, R.4
  • 22
    • 0342424729 scopus 로고    scopus 로고
    • A small protein that mediates the activation of a two-component system by another two-component system
    • Kox L.F., Wosten M.M., Groisman E.A. A small protein that mediates the activation of a two-component system by another two-component system. EMBO J. 2000, 19:1861-1872.
    • (2000) EMBO J. , vol.19 , pp. 1861-1872
    • Kox, L.F.1    Wosten, M.M.2    Groisman, E.A.3
  • 23
    • 0037310768 scopus 로고    scopus 로고
    • RmpA2, an activator of capsule biosynthesis in Klebsiella pneumoniae CG43, regulates K2 cps gene expression at the transcriptional level
    • Lai Y.C., Peng H.L., Chang H.Y. RmpA2, an activator of capsule biosynthesis in Klebsiella pneumoniae CG43, regulates K2 cps gene expression at the transcriptional level. J. Bacteriol. 2003, 185:788-800.
    • (2003) J. Bacteriol. , vol.185 , pp. 788-800
    • Lai, Y.C.1    Peng, H.L.2    Chang, H.Y.3
  • 24
    • 38449103508 scopus 로고    scopus 로고
    • NMR methods for studying protein-protein interactions involved in translation initiation
    • Marintchev A., Frueh D., Wagner G. NMR methods for studying protein-protein interactions involved in translation initiation. Methods Enzymol. 2007, 430:283-331.
    • (2007) Methods Enzymol. , vol.430 , pp. 283-331
    • Marintchev, A.1    Frueh, D.2    Wagner, G.3
  • 25
    • 53549100745 scopus 로고    scopus 로고
    • Signal integration in bacterial two-component regulatory systems
    • Mitrophanov A.Y., Groisman E.A. Signal integration in bacterial two-component regulatory systems. Genes Dev. 2008, 22:2601-2611.
    • (2008) Genes Dev. , vol.22 , pp. 2601-2611
    • Mitrophanov, A.Y.1    Groisman, E.A.2
  • 28
    • 5144231590 scopus 로고    scopus 로고
    • Solution structure of the Escherichia coli YojN histidine-phosphotransferase domain and its interaction with cognate phosphoryl receiver domains
    • Rogov V.V., Bernhard F., Lohr F., Dotsch V. Solution structure of the Escherichia coli YojN histidine-phosphotransferase domain and its interaction with cognate phosphoryl receiver domains. J. Mol. Biol. 2004, 343:1035-1048.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1035-1048
    • Rogov, V.V.1    Bernhard, F.2    Lohr, F.3    Dotsch, V.4
  • 29
    • 33750336664 scopus 로고    scopus 로고
    • A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains
    • Rogov V.V., Rogova N.Y., Bernhard F., Koglin A., Lohr F., Dotsch V. A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains. J. Mol. Biol. 2006, 364:68-79.
    • (2006) J. Mol. Biol. , vol.364 , pp. 68-79
    • Rogov, V.V.1    Rogova, N.Y.2    Bernhard, F.3    Koglin, A.4    Lohr, F.5    Dotsch, V.6
  • 31
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Roman A.L., Rullmann J.A.C., Malcolm W.M., Robert K., Janet M.T. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 1996, V8:477-486.
    • (1996) J. Biomol. NMR , vol.V8 , pp. 477-486
    • Roman, A.L.1    Rullmann, J.A.C.2    Malcolm, W.M.3    Robert, K.4    Janet, M.T.5
  • 34
    • 0034051065 scopus 로고    scopus 로고
    • A novel NMR method for determining the interfaces of large protein-protein complexes
    • Takahashi H., Nakanishi T., Kami K., Arata Y., Shimada I. A novel NMR method for determining the interfaces of large protein-protein complexes. Nat. Struct. Biol. 2000, 7:220-223.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 220-223
    • Takahashi, H.1    Nakanishi, T.2    Kami, K.3    Arata, Y.4    Shimada, I.5
  • 36
    • 10344224043 scopus 로고    scopus 로고
    • Phenotypic differences between Salmonella and Escherichia coli resulting from the disparate regulation of homologous genes
    • Winfield M.D., Groisman E.A. Phenotypic differences between Salmonella and Escherichia coli resulting from the disparate regulation of homologous genes. Proc. Natl. Acad. Sci. USA 2004, 101:17162-17167.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17162-17167
    • Winfield, M.D.1    Groisman, E.A.2
  • 37
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart D.S., Sykes B.D. The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR 1994, 4:171-180.
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 38
  • 39
    • 0030953080 scopus 로고    scopus 로고
    • Two-component signal transducers and MAPK cascades
    • Wurgler-Murphy S.M., Saito H. Two-component signal transducers and MAPK cascades. Trends Biochem. Sci. 1997, 22:172-176.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 172-176
    • Wurgler-Murphy, S.M.1    Saito, H.2
  • 41
    • 0034662751 scopus 로고    scopus 로고
    • A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction
    • Zapf J., Sen U., Madhusudan, Hoch J.A., Varughese K.I. A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction. Structure 2000, 8:851-862.
    • (2000) Structure , vol.8 , pp. 851-862
    • Zapf, J.1    Sen, U.2    Madhusudan3    Hoch, J.A.4    Varughese, K.I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.