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Volumn 425, Issue 12, 2013, Pages 2219-2231

Ligand binding reduces conformational flexibility in the active site of tyrosine phosphatase related to biofilm formation A (TpbA) from pseudomonas aeruginosa

Author keywords

bacterial signaling; dual specificity phosphatase; NMR spectroscopy; open closed state active site dynamics; Pseudomonas aeruginosa

Indexed keywords

PROTEIN TYROSINE PHOSPHATASE;

EID: 84878217023     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.03.023     Document Type: Article
Times cited : (16)

References (46)
  • 2
    • 0028359370 scopus 로고
    • PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
    • R.H. Diamond, D.E. Cressman, T.M. Laz, C.S. Abrams, and R. Taub PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth Mol. Cell. Biol. 14 1994 3752 3762
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3752-3762
    • Diamond, R.H.1    Cressman, D.E.2    Laz, T.M.3    Abrams, C.S.4    Taub, R.5
  • 3
    • 18144384775 scopus 로고    scopus 로고
    • Essential role for mitogen-activated protein (MAP) kinase phosphatase-1 in stress-responsive MAP kinase and cell survival signaling
    • J.J. Wu, and A.M. Bennett Essential role for mitogen-activated protein (MAP) kinase phosphatase-1 in stress-responsive MAP kinase and cell survival signaling J. Biol. Chem. 280 2005 16461 16466
    • (2005) J. Biol. Chem. , vol.280 , pp. 16461-16466
    • Wu, J.J.1    Bennett, A.M.2
  • 4
    • 33845693412 scopus 로고    scopus 로고
    • Diverse physiological functions for dual-specificity MAP kinase phosphatases
    • R.J. Dickinson, and S.M. Keyse Diverse physiological functions for dual-specificity MAP kinase phosphatases J. Cell Sci. 119 2006 4607 4615
    • (2006) J. Cell Sci. , vol.119 , pp. 4607-4615
    • Dickinson, R.J.1    Keyse, S.M.2
  • 5
    • 79954424659 scopus 로고    scopus 로고
    • Shigella flexneri type III secreted effector OspF reveals new crosstalks of proinflammatory signaling pathways during bacterial infection
    • V. Reiterer, L. Grossniklaus, T. Tschon, C.A. Kasper, I. Sorg, and C. Arrieumerlou Shigella flexneri type III secreted effector OspF reveals new crosstalks of proinflammatory signaling pathways during bacterial infection Cell. Signal. 23 2011 1188 1196
    • (2011) Cell. Signal. , vol.23 , pp. 1188-1196
    • Reiterer, V.1    Grossniklaus, L.2    Tschon, T.3    Kasper, C.A.4    Sorg, I.5    Arrieumerlou, C.6
  • 6
    • 67650863623 scopus 로고    scopus 로고
    • Connecting quorum sensing, c-di-GMP, pel polysaccharide, and biofilm formation in Pseudomonas aeruginosa through tyrosine phosphatase TpbA (PA3885)
    • A. Ueda, and T.K. Wood Connecting quorum sensing, c-di-GMP, pel polysaccharide, and biofilm formation in Pseudomonas aeruginosa through tyrosine phosphatase TpbA (PA3885) PLoS Pathog. 5 2009 e1000483
    • (2009) PLoS Pathog. , vol.5 , pp. 1000483
    • Ueda, A.1    Wood, T.K.2
  • 8
    • 0348230977 scopus 로고    scopus 로고
    • The application of biofilm science to the study and control of chronic bacterial infections
    • W. Costerton, R. Veeh, M. Shirtliff, M. Pasmore, C. Post, and G. Ehrlich The application of biofilm science to the study and control of chronic bacterial infections J. Clin. Invest. 112 2003 1466 1477
    • (2003) J. Clin. Invest. , vol.112 , pp. 1466-1477
    • Costerton, W.1    Veeh, R.2    Shirtliff, M.3    Pasmore, M.4    Post, C.5    Ehrlich, G.6
  • 9
    • 78149464873 scopus 로고    scopus 로고
    • Tyrosine phosphatase TpbA controls rugose colony formation in Pseudomonas aeruginosa by dephosphorylating diguanylate cyclase TpbB
    • M. Pu, and T.K. Wood Tyrosine phosphatase TpbA controls rugose colony formation in Pseudomonas aeruginosa by dephosphorylating diguanylate cyclase TpbB Biochem. Biophys. Res. Commun. 402 2010 351 355
    • (2010) Biochem. Biophys. Res. Commun. , vol.402 , pp. 351-355
    • Pu, M.1    Wood, T.K.2
  • 10
    • 0029043627 scopus 로고
    • A catalytic mechanism for the dual-specific phosphatases
    • J.M. Denu, and J.E. Dixon A catalytic mechanism for the dual-specific phosphatases Proc. Natl Acad. Sci. USA 92 1995 5910 5914
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5910-5914
    • Denu, J.M.1    Dixon, J.E.2
  • 11
    • 0031860103 scopus 로고    scopus 로고
    • The structure and mechanism of protein phosphatases: Insights into catalysis and regulation
    • D. Barford, A.K. Das, and M.P. Egloff The structure and mechanism of protein phosphatases: insights into catalysis and regulation Annu. Rev. Biophys. Biomol. Struct. 27 1998 133 164
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 133-164
    • Barford, D.1    Das, A.K.2    Egloff, M.P.3
  • 12
    • 84874958147 scopus 로고    scopus 로고
    • Backbone and sidechain (1)H, (15)N and (13)C assignments of tyrosine phosphatase related to biofilm formation A (TpbA) of Pseudomonas aeruginosa
    • D. Koveal, T.B. Jayasundera, T.K. Wood, W. Peti, and R. Page Backbone and sidechain (1)H, (15)N and (13)C assignments of tyrosine phosphatase related to biofilm formation A (TpbA) of Pseudomonas aeruginosa Biomol. NMR Assign. 7 2013 57 59
    • (2013) Biomol. NMR Assign. , vol.7 , pp. 57-59
    • Koveal, D.1    Jayasundera, T.B.2    Wood, T.K.3    Peti, W.4    Page, R.5
  • 14
    • 21044449889 scopus 로고    scopus 로고
    • RECOORD: A recalculated coordinate database of 500 + proteins from the PDB using restraints from the BioMagResBank
    • A.J. Nederveen, J.F. Doreleijers, W. Vranken, Z. Miller, C.A. Spronk, and S.B. Nabuurs RECOORD: a recalculated coordinate database of 500 + proteins from the PDB using restraints from the BioMagResBank Proteins 59 2005 662 672
    • (2005) Proteins , vol.59 , pp. 662-672
    • Nederveen, A.J.1    Doreleijers, J.F.2    Vranken, W.3    Miller, Z.4    Spronk, C.A.5    Nabuurs, S.B.6
  • 15
    • 68949170804 scopus 로고    scopus 로고
    • Structural analysis of a multifunctional, tandemly repeated inositol polyphosphatase
    • R.J. Gruninger, L.B. Selinger, and S.C. Mosimann Structural analysis of a multifunctional, tandemly repeated inositol polyphosphatase J. Mol. Biol. 392 2009 75 86
    • (2009) J. Mol. Biol. , vol.392 , pp. 75-86
    • Gruninger, R.J.1    Selinger, L.B.2    Mosimann, S.C.3
  • 16
    • 7944229708 scopus 로고    scopus 로고
    • Structures of Selenomonas ruminantium phytase in complex with persulfated phytate: DSP phytase fold and mechanism for sequential substrate hydrolysis
    • H.M. Chu, R.T. Guo, T.W. Lin, C.C. Chou, H.L. Shr, and H.L. Lai Structures of Selenomonas ruminantium phytase in complex with persulfated phytate: DSP phytase fold and mechanism for sequential substrate hydrolysis Structure 12 2004 2015 2024
    • (2004) Structure , vol.12 , pp. 2015-2024
    • Chu, H.M.1    Guo, R.T.2    Lin, T.W.3    Chou, C.C.4    Shr, H.L.5    Lai, H.L.6
  • 17
    • 34250815835 scopus 로고    scopus 로고
    • Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase
    • A.A. Puhl, R.J. Gruninger, R. Greiner, T.W. Janzen, S.C. Mosimann, and L.B. Selinger Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase Protein Sci. 16 2007 1368 1378
    • (2007) Protein Sci. , vol.16 , pp. 1368-1378
    • Puhl, A.A.1    Gruninger, R.J.2    Greiner, R.3    Janzen, T.W.4    Mosimann, S.C.5    Selinger, L.B.6
  • 19
    • 0035844140 scopus 로고    scopus 로고
    • Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1
    • D.N. Slack, O.M. Seternes, M. Gabrielsen, and S.M. Keyse Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1 J. Biol. Chem. 276 2001 16491 16500
    • (2001) J. Biol. Chem. , vol.276 , pp. 16491-16500
    • Slack, D.N.1    Seternes, O.M.2    Gabrielsen, M.3    Keyse, S.M.4
  • 20
    • 0037177212 scopus 로고    scopus 로고
    • Design and characterization of an improved protein tyrosine phosphatase substrate-trapping mutant
    • L. Xie, Y.L. Zhang, and Z.Y. Zhang Design and characterization of an improved protein tyrosine phosphatase substrate-trapping mutant Biochemistry 41 2002 4032 4039
    • (2002) Biochemistry , vol.41 , pp. 4032-4039
    • Xie, L.1    Zhang, Y.L.2    Zhang, Z.Y.3
  • 21
    • 0031055324 scopus 로고    scopus 로고
    • Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases
    • A.J. Flint, T. Tiganis, D. Barford, and N.K. Tonks Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases Proc. Natl Acad. Sci. USA 94 1997 1680 1685
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1680-1685
    • Flint, A.J.1    Tiganis, T.2    Barford, D.3    Tonks, N.K.4
  • 22
    • 0032910476 scopus 로고    scopus 로고
    • Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation
    • A.E. Stewart, S. Dowd, S.M. Keyse, and N.Q. McDonald Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation Nat. Struct. Biol. 6 1999 174 181
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 174-181
    • Stewart, A.E.1    Dowd, S.2    Keyse, S.M.3    McDonald, N.Q.4
  • 23
    • 1642482862 scopus 로고    scopus 로고
    • Structural insights into molecular function of the metastasis-associated phosphatase PRL-3
    • G. Kozlov, J. Cheng, E. Ziomek, D. Banville, K. Gehring, and I. Ekiel Structural insights into molecular function of the metastasis-associated phosphatase PRL-3 J. Biol. Chem. 279 2004 11882 11889
    • (2004) J. Biol. Chem. , vol.279 , pp. 11882-11889
    • Kozlov, G.1    Cheng, J.2    Ziomek, E.3    Banville, D.4    Gehring, K.5    Ekiel, I.6
  • 24
    • 35748973537 scopus 로고    scopus 로고
    • A novel phosphatase family, structurally related to dual-specificity phosphatases, that displays unique amino acid sequence and substrate specificity
    • C. Roma-Mateo, P. Rios, L. Tabernero, T.K. Attwood, and R. Pulido A novel phosphatase family, structurally related to dual-specificity phosphatases, that displays unique amino acid sequence and substrate specificity J. Mol. Biol. 374 2007 899 909
    • (2007) J. Mol. Biol. , vol.374 , pp. 899-909
    • Roma-Mateo, C.1    Rios, P.2    Tabernero, L.3    Attwood, T.K.4    Pulido, R.5
  • 25
    • 44049092771 scopus 로고    scopus 로고
    • Structure of human dual specificity protein phosphatase 23, VHZ, enzyme-substrate/product complex
    • R. Agarwal, S.K. Burley, and S. Swaminathan Structure of human dual specificity protein phosphatase 23, VHZ, enzyme-substrate/product complex J. Biol. Chem. 283 2008 8946 8953
    • (2008) J. Biol. Chem. , vol.283 , pp. 8946-8953
    • Agarwal, R.1    Burley, S.K.2    Swaminathan, S.3
  • 26
    • 0041312681 scopus 로고    scopus 로고
    • The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase
    • C.H. Gray, V.M. Good, N.K. Tonks, and D. Barford The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase EMBO J. 22 2003 3524 3535
    • (2003) EMBO J. , vol.22 , pp. 3524-3535
    • Gray, C.H.1    Good, V.M.2    Tonks, N.K.3    Barford, D.4
  • 29
    • 2342658395 scopus 로고    scopus 로고
    • Structure of human PRL-3, the phosphatase associated with cancer metastasis
    • K.A. Kim, J.S. Song, J. Jee, M.R. Sheen, C. Lee, and T.G. Lee Structure of human PRL-3, the phosphatase associated with cancer metastasis FEBS Lett. 565 2004 181 187
    • (2004) FEBS Lett. , vol.565 , pp. 181-187
    • Kim, K.A.1    Song, J.S.2    Jee, J.3    Sheen, M.R.4    Lee, C.5    Lee, T.G.6
  • 30
    • 77953719742 scopus 로고    scopus 로고
    • Solution structure and conformational heterogeneity of acylphosphatase from Bacillus subtilis
    • J. Hu, D. Li, X.D. Su, C. Jin, and B. Xia Solution structure and conformational heterogeneity of acylphosphatase from Bacillus subtilis FEBS Lett. 584 2010 2852 2856
    • (2010) FEBS Lett. , vol.584 , pp. 2852-2856
    • Hu, J.1    Li, D.2    Su, X.D.3    Jin, C.4    Xia, B.5
  • 31
    • 0037317607 scopus 로고    scopus 로고
    • Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP
    • A. Farooq, O. Plotnikova, G. Chaturvedi, S. Yan, L. Zeng, Q. Zhang, and M.M. Zhou Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP Structure 11 2003 155 164
    • (2003) Structure , vol.11 , pp. 155-164
    • Farooq, A.1    Plotnikova, O.2    Chaturvedi, G.3    Yan, S.4    Zeng, L.5    Zhang, Q.6    Zhou, M.M.7
  • 32
    • 84867280562 scopus 로고    scopus 로고
    • The apo-structure of the low molecular weight protein-tyrosine phosphatase A (MptpA) from Mycobacterium tuberculosis allows for better target-specific drug development
    • T. Stehle, S. Sreeramulu, F. Lohr, C. Richter, K. Saxena, H.R. Jonker, and H. Schwalbe The apo-structure of the low molecular weight protein-tyrosine phosphatase A (MptpA) from Mycobacterium tuberculosis allows for better target-specific drug development J. Biol. Chem. 287 2012 34569 34582
    • (2012) J. Biol. Chem. , vol.287 , pp. 34569-34582
    • Stehle, T.1    Sreeramulu, S.2    Lohr, F.3    Richter, C.4    Saxena, K.5    Jonker, H.R.6    Schwalbe, H.7
  • 33
    • 33845675681 scopus 로고    scopus 로고
    • Crystal structure of human TMDP, a testis-specific dual specificity protein phosphatase: Implications for substrate specificity
    • S.J. Kim, D.G. Jeong, T.S. Yoon, J.H. Son, S.K. Cho, S.E. Ryu, and J.H. Kim Crystal structure of human TMDP, a testis-specific dual specificity protein phosphatase: implications for substrate specificity Proteins 66 2007 239 245
    • (2007) Proteins , vol.66 , pp. 239-245
    • Kim, S.J.1    Jeong, D.G.2    Yoon, T.S.3    Son, J.H.4    Cho, S.K.5    Ryu, S.E.6    Kim, J.H.7
  • 34
    • 33745968271 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human MAP kinase phosphatase 5: Structural insight into constitutively active phosphatase
    • D.G. Jeong, T.S. Yoon, J.H. Kim, M.Y. Shim, S.K. Jung, and J.H. Son Crystal structure of the catalytic domain of human MAP kinase phosphatase 5: structural insight into constitutively active phosphatase J. Mol. Biol. 360 2006 946 955
    • (2006) J. Mol. Biol. , vol.360 , pp. 946-955
    • Jeong, D.G.1    Yoon, T.S.2    Kim, J.H.3    Shim, M.Y.4    Jung, S.K.5    Son, J.H.6
  • 35
    • 0029975476 scopus 로고    scopus 로고
    • Crystal structure of the dual specificity protein phosphatase VHR
    • J. Yuvaniyama, J.M. Denu, J.E. Dixon, and M.A. Saper Crystal structure of the dual specificity protein phosphatase VHR Science 272 1996 1328 1331
    • (1996) Science , vol.272 , pp. 1328-1331
    • Yuvaniyama, J.1    Denu, J.M.2    Dixon, J.E.3    Saper, M.A.4
  • 36
    • 0037028988 scopus 로고    scopus 로고
    • An effective method for the discrimination of motional anisotropy and chemical exchange
    • J.M. Kneller, M. Lu, and C. Bracken An effective method for the discrimination of motional anisotropy and chemical exchange J. Am. Chem. Soc. 124 2002 1852 1853
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1852-1853
    • Kneller, J.M.1    Lu, M.2    Bracken, C.3
  • 37
    • 25844459468 scopus 로고    scopus 로고
    • Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop
    • C.L. Gustafson, C.V. Stauffacher, K. Hallenga, and R.L. Van Etten Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop Protein Sci. 14 2005 2515 2525
    • (2005) Protein Sci. , vol.14 , pp. 2515-2525
    • Gustafson, C.L.1    Stauffacher, C.V.2    Hallenga, K.3    Van Etten, R.L.4
  • 39
    • 4143132362 scopus 로고    scopus 로고
    • The minimal essential core of a cysteine-based protein-tyrosine phosphatase revealed by a novel 16-kDa VH1-like phosphatase, VHZ
    • A. Alonso, S. Burkhalter, J. Sasin, L. Tautz, J. Bogetz, and H. Huynh The minimal essential core of a cysteine-based protein-tyrosine phosphatase revealed by a novel 16-kDa VH1-like phosphatase, VHZ J. Biol. Chem. 279 2004 35768 35774
    • (2004) J. Biol. Chem. , vol.279 , pp. 35768-35774
    • Alonso, A.1    Burkhalter, S.2    Sasin, J.3    Tautz, L.4    Bogetz, J.5    Huynh, H.6
  • 40
    • 84870872419 scopus 로고    scopus 로고
    • New aspects of the phosphatase VHZ revealed by a high-resolution structure with vanadate and substrate screening
    • V.I. Kuznetsov, A.C. Hengge, and S.J. Johnson New aspects of the phosphatase VHZ revealed by a high-resolution structure with vanadate and substrate screening Biochemistry 51 2012 9869 9879
    • (2012) Biochemistry , vol.51 , pp. 9869-9879
    • Kuznetsov, V.I.1    Hengge, A.C.2    Johnson, S.J.3
  • 41
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • P. Guntert Automated NMR structure calculation with CYANA Methods Mol. Biol. 278 2004 353 378
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Guntert, P.1
  • 42
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • T. Herrmann, P. Guntert, and K. Wuthrich Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS J. Biomol. NMR 24 2002 171 189
    • (2002) J. Biomol. NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 43
    • 68349093958 scopus 로고    scopus 로고
    • TALOS +: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Y. Shen, F. Delaglio, G. Cornilescu, and A. Bax TALOS +: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts J. Biomol. NMR 44 2009 213 223
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 45
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    Macarthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 46
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graphics 14 1996 29 32
    • (1996) J. Mol. Graphics , vol.14 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


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