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Volumn 288, Issue 21, 2013, Pages 14863-14873

The cation-π box is a specific phosphatidylcholine membrane targeting motif

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSOLIC PROTEINS; MOLECULAR DETERMINANTS; PERIPHERAL MEMBRANES; PERIPHERAL PROTEINS; PHOSPHATIDYLCHOLINE; SECONDARY STRUCTURES; SPECIFIC RECOGNITION; STAPHYLOCOCCUS AUREUS;

EID: 84878249753     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.466532     Document Type: Article
Times cited : (40)

References (41)
  • 2
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon, M. A. (2008) Membrane recognition by phospholipid-binding domains. Nat. Rev. Mol. Cell Biol. 9, 99-111
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 3
    • 77953762012 scopus 로고    scopus 로고
    • Translation of the phosphoinositide code by PI effectors
    • Kutateladze, T. G. (2010) Translation of the phosphoinositide code by PI effectors. Nat. Chem. Biol. 6, 507-513
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 507-513
    • Kutateladze, T.G.1
  • 4
    • 84864337089 scopus 로고    scopus 로고
    • Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs, a β-propeller protein family
    • Krick, R., Busse, R. A., Scacioc, A., Stephan, M., Janshoff, A., Thumm, M., and Kühnel, K. (2012) Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs, a β-propeller protein family. Proc. Natl. Acad. Sci. U.S.A. 109, E2042-E2049
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109
    • Krick, R.1    Busse, R.A.2    Scacioc, A.3    Stephan, M.4    Janshoff, A.5    Thumm, M.6    Kühnel, K.7
  • 7
    • 43749112983 scopus 로고    scopus 로고
    • Crystal structure of lactadherin C2 domain at 1.7-Å resolution with mutational and computational analyses of its membrane binding motif
    • Shao, C., Novakovic, V. A., Head, J. F., Seaton, B. A., and Gilbert, G. E. (2008) Crystal structure of lactadherin C2 domain at 1.7-Å resolution with mutational and computational analyses of its membrane binding motif. J. Biol. Chem. 283, 7230-7241
    • (2008) J. Biol. Chem. , vol.283 , pp. 7230-7241
    • Shao, C.1    Novakovic, V.A.2    Head, J.F.3    Seaton, B.A.4    Gilbert, G.E.5
  • 8
    • 0037205478 scopus 로고    scopus 로고
    • Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C
    • DOI 10.1074/jbc.M200938200
    • Feng, J., Wehbi, H., and Roberts, M. F. (2002) Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C. J. Biol. Chem. 277, 19867-19875 (Pubitemid 34967506)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.22 , pp. 19867-19875
    • Feng, J.1    Wehbi, H.2    Roberts, M.F.3
  • 9
    • 78249261241 scopus 로고    scopus 로고
    • Single molecule diffusion of membrane-bound proteins. Window into lipid contacts and bilayer dynamics
    • Knight, J. D., Lerner, M. G., Marcano-Velázquez, J. G., Pastor, R. W., and Falke, J. J. (2010) Single molecule diffusion of membrane-bound proteins. Window into lipid contacts and bilayer dynamics. Biophys. J. 99, 2879-2887
    • (2010) Biophys. J. , vol.99 , pp. 2879-2887
    • Knight, J.D.1    Lerner, M.G.2    Marcano-Velázquez, J.G.3    Pastor, R.W.4    Falke, J.J.5
  • 10
    • 0030847158 scopus 로고    scopus 로고
    • Allosteric activation of phosphatidylinositol-specific phospholipase C: Specific phospholipid binding anchors the enzyme to the interface
    • DOI 10.1021/bi970846o
    • Zhou, C., Qian, X., and Roberts, M. F. (1997) Allosteric activation of phosphatidylinositol-specific phospholipase C. Specific phospholipid binding anchors the enzyme to the interface. Biochemistry 36, 10089-10097 (Pubitemid 27357717)
    • (1997) Biochemistry , vol.36 , Issue.33 , pp. 10089-10097
    • Zhou, C.1    Qian, X.2    Roberts, M.F.3
  • 11
    • 1242339645 scopus 로고    scopus 로고
    • Cation-π Interactions as Determinants for Binding of the Compatible Solutes Glycine Betaine and Proline Betaine by the Periplasmic Ligand-binding Protein ProX from Escherichia coli
    • DOI 10.1074/jbc.M309771200
    • Schiefner, A., Breed, J., Bösser, L., Kneip, S., Gade, J., Holtmann, G., Diederichs, K., Welte, W., and Bremer, E. (2004) Cation-π interactions as determinants for binding of the compatible solutes glycine betaine and proline betaine by the periplasmic ligand-binding protein ProX from Escherichia coli. J. Biol. Chem. 279, 5588-5596 (Pubitemid 38220585)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5588-5596
    • Schiefner, A.1    Breed, J.2    Bosser, L.3    Kneip, S.4    Gade, J.5    Holtmann, G.6    Diederichs, K.7    Welte, W.8    Bremer, E.9
  • 12
    • 79960697231 scopus 로고    scopus 로고
    • Arg149 is involved in switching the low affinity, open state of the binding protein AfProX into its high affinity, closed state
    • Tschapek, B., Pittelkow, M., Sohn-Bösser, L., Holtmann, G., Smits, S. H., Gohlke, H., Bremer, E., and Schmitt, L. (2011) Arg149 is involved in switching the low affinity, open state of the binding protein AfProX into its high affinity, closed state. J. Mol. Biol. 411, 36-52
    • (2011) J. Mol. Biol. , vol.411 , pp. 36-52
    • Tschapek, B.1    Pittelkow, M.2    Sohn-Bösser, L.3    Holtmann, G.4    Smits, S.H.5    Gohlke, H.6    Bremer, E.7    Schmitt, L.8
  • 13
    • 57749122030 scopus 로고    scopus 로고
    • Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states
    • Oswald, C., Smits, S. H., Höing, M., Sohn-Bösser, L., Dupont, L., Le Rudulier, D., Schmitt, L., and Bremer, E. (2008) Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states. J. Biol. Chem. 283, 32848-32859
    • (2008) J. Biol. Chem. , vol.283 , pp. 32848-32859
    • Oswald, C.1    Smits, S.H.2    Höing, M.3    Sohn-Bösser, L.4    Dupont, L.5    Le Rudulier, D.6    Schmitt, L.7    Bremer, E.8
  • 14
    • 79960698795 scopus 로고    scopus 로고
    • The crystal structure of the substrate-binding protein OpuBC from Bacillus subtilis in complex with choline
    • Pittelkow, M., Tschapek, B., Smits, S. H., Schmitt, L., and Bremer, E. (2011) The crystal structure of the substrate-binding protein OpuBC from Bacillus subtilis in complex with choline. J. Mol. Biol. 411, 53-67
    • (2011) J. Mol. Biol. , vol.411 , pp. 53-67
    • Pittelkow, M.1    Tschapek, B.2    Smits, S.H.3    Schmitt, L.4    Bremer, E.5
  • 16
    • 0037086355 scopus 로고    scopus 로고
    • Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail
    • DOI 10.1126/science.1069473
    • Jacobs, S. A., and Khorasanizadeh, S. (2002) Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295, 2080-2083 (Pubitemid 34229471)
    • (2002) Science , vol.295 , Issue.5562 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 17
    • 40949148102 scopus 로고    scopus 로고
    • The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules
    • DOI 10.1038/nsmb.1384, PII NSMB1384
    • Collins, R. E., Northrop, J. P., Horton, J. R., Lee, D. Y., Zhang, X., Stallcup, M. R., and Cheng, X. (2008) The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules. Nat. Struct. Mol. Biol. 15, 245-250 (Pubitemid 351654039)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.3 , pp. 245-250
    • Collins, R.E.1    Northrop, J.P.2    Horton, J.R.3    Lee, D.Y.4    Zhang, X.5    Stallcup, M.R.6    Cheng, X.7
  • 20
    • 0031691667 scopus 로고    scopus 로고
    • Localization of putative virulence genes on a physical map of the bacillus thuringiensis subsp. gelechiae chromosome
    • DOI 10.1007/s002849900373
    • Lovgren, A., Carlson, C. R., Eskils, K., and Kolsto, A. B. (1998) Localization of putative virulence genes on a physical map of the Bacillus thuringiensis subsp. gelechiae chromosome. Curr. Microbiol. 37, 245-250 (Pubitemid 28433825)
    • (1998) Current Microbiology , vol.37 , Issue.4 , pp. 245-250
    • Lovgren, A.1    Carlson, C.R.2    Eskils, K.3    Kolsto, A.-B.4
  • 21
    • 0027360072 scopus 로고
    • Cloning, expression, and mutagenesis of phosphatidylinositol-specific phospholipase C from Staphylococcus aureus: A potential staphylococcal virulence factor
    • Daugherty, S., and Low, M. G. (1993) Cloning, expression, and mutagenesis of phosphatidylinositol-specificphospholipaseCfrom Staphylococcusaureus. Apotential staphylococcal virulence factor. Infect. Immun. 61, 5078-5089 (Pubitemid 23353883)
    • (1993) Infection and Immunity , vol.61 , Issue.12 , pp. 5078-5089
    • Daugherty, S.1    Low, M.G.2
  • 22
    • 77956256450 scopus 로고    scopus 로고
    • Defining specific lipid binding sites for a peripheral membrane protein in situ using subtesla field cycling NMR
    • Pu, M., Orr, A., Redfield, A. G., and Roberts, M. F. (2010) Defining specific lipid binding sites for a peripheral membrane protein in situ using subtesla field cycling NMR. J. Biol. Chem. 285, 26916-26922
    • (2010) J. Biol. Chem. , vol.285 , pp. 26916-26922
    • Pu, M.1    Orr, A.2    Redfield, A.G.3    Roberts, M.F.4
  • 23
    • 84870038612 scopus 로고    scopus 로고
    • Competition between anion binding and dimerization modulates S. aureus phosphatidylinositol-specific phospholipase C enzymatic activity
    • Cheng, J., Goldstein, R., Stec, B., Gershenson, A., and Roberts, M. F. (2012) Competition between anion binding and dimerization modulates S. aureus phosphatidylinositol-specific phospholipase C enzymatic activity. J. Biol. Chem. 287, 40317-40327
    • (2012) J. Biol. Chem. , vol.287 , pp. 40317-40327
    • Cheng, J.1    Goldstein, R.2    Stec, B.3    Gershenson, A.4    Roberts, M.F.5
  • 24
    • 84859193467 scopus 로고    scopus 로고
    • Structure of the S. aureus PI-specific phospholipase C reveals modulation of active site access by a titratable π-cation latched loop
    • Goldstein, R., Cheng, J., Stec, B., and Roberts, M. F. (2012) Structure of the S. aureus PI-specific phospholipase C reveals modulation of active site access by a titratable π-cation latched loop. Biochemistry 51, 2579-2587
    • (2012) Biochemistry , vol.51 , pp. 2579-2587
    • Goldstein, R.1    Cheng, J.2    Stec, B.3    Roberts, M.F.4
  • 25
    • 67651230535 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy of phosphatidylinositol-specific phospholipase C monitors the interplay of substrate and activator lipid binding
    • Pu, M., Roberts, M. F., and Gershenson, A. (2009) Fluorescence correlation spectroscopy of phosphatidylinositol-specific phospholipase C monitors the interplay of substrate and activator lipid binding. Biochemistry 48, 6835-6845
    • (2009) Biochemistry , vol.48 , pp. 6835-6845
    • Pu, M.1    Roberts, M.F.2    Gershenson, A.3
  • 27
    • 0041571480 scopus 로고    scopus 로고
    • Investigating the interfacial binding of bacterial phosphatidylinositol- specific phospholipase C
    • DOI 10.1021/bi034195+
    • Wehbi, H., Feng, J., Kolbeck, J., Ananthanarayanan, B., Cho, W., and Roberts, M. F. (2003) Investigating the interfacial binding of bacterial phos-phatidylinositol- specific phospholipase C. Biochemistry 42, 9374-9382 (Pubitemid 36959245)
    • (2003) Biochemistry , vol.42 , Issue.31 , pp. 9374-9382
    • Wehbi, H.1    Feng, J.2    Kolbeck, J.3    Ananthanarayanan, B.4    Cho, W.5    Roberts, M.F.6
  • 28
    • 67650123206 scopus 로고    scopus 로고
    • Modulation of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface
    • Shi, X., Shao, C., Zhang, X., Zambonelli, C., Redfield, A. G., Head, J. F., Seaton, B. A., and Roberts, M. F. (2009) Modulation of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface. J. Biol. Chem. 284, 15607-15618
    • (2009) J. Biol. Chem. , vol.284 , pp. 15607-15618
    • Shi, X.1    Shao, C.2    Zhang, X.3    Zambonelli, C.4    Redfield, A.G.5    Head, J.F.6    Seaton, B.A.7    Roberts, M.F.8
  • 29
    • 84860202526 scopus 로고    scopus 로고
    • High-resolution NMR field cycling device for full range relaxation and structural studies of biopolymers on a shared commercial instrument
    • Redfield, A. G. (2012) High-resolution NMR field cycling device for full range relaxation and structural studies of biopolymers on a shared commercial instrument. J. Biomol. NMR 52, 159-177
    • (2012) J. Biomol. NMR , vol.52 , pp. 159-177
    • Redfield, A.G.1
  • 30
    • 0001428858 scopus 로고
    • Thermodynamic comparison of lysoand diacylphosphatidylcholines
    • Bian, J., and Roberts, M. F. (1992) Thermodynamic comparison of lysoand diacylphosphatidylcholines. J. Colloid. Interface Sci. 153, 420-428
    • (1992) J. Colloid. Interface Sci. , vol.153 , pp. 420-428
    • Bian, J.1    Roberts, M.F.2
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 0028103275 scopus 로고
    • The CCP4 Suite. Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 Suite. Programs for protein crystallography. Acta Crystallogr.DBiol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr.DBiol. Crystallogr. , vol.50 , pp. 760-763
  • 36
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • Krissinel, E., and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60, 2256-2268 (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 I , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 37
    • 0000243829 scopus 로고
    • PROCHECK. A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK. A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 38
    • 0029121937 scopus 로고
    • Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol
    • Heinz, D. W., Ryan, M., Bullock, T. L., and Griffith, O. H. (1995) Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol. EMBO J. 14, 3855-3863
    • (1995) EMBO J. , vol.14 , pp. 3855-3863
    • Heinz, D.W.1    Ryan, M.2    Bullock, T.L.3    Griffith, O.H.4
  • 39
    • 0031576330 scopus 로고    scopus 로고
    • Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenes
    • DOI 10.1006/jmbi.1997.1290
    • Moser, J., Gerstel, B., Meyer, J. E., Chakraborty, T., Wehland, J., and Heinz, D. W. (1997) Crystal structure of the phosphatidylinositolspecific phospholipase C from the human pathogen, Listeria monocytogenes. J. Mol. Biol. 273, 269-282 (Pubitemid 27460229)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.1 , pp. 269-282
    • Moser, J.1    Gerstel, B.2    Meyer, J.E.W.3    Chakraborty, T.4    Wehland, J.5    Heinz, D.W.6
  • 40
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • DOI 10.1038/nsb1096-842
    • Wimley, W. C., and White, S. H. (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3, 842-848 (Pubitemid 26330634)
    • (1996) Nature Structural Biology , vol.3 , Issue.10 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 41
    • 84876493429 scopus 로고    scopus 로고
    • Cation-π interactions as lipid-specific anchors for phos-phatidylinositol-specific phospholipase-C
    • Grauffel, C., Yang, B., He, T., Roberts, M. F., Gershenson, A., and Reuter, N. (2013) Cation-π interactions as lipid-specific anchors for phos-phatidylinositol-specific phospholipase-C. J. Am. Chem. Soc. 135, 5740 -5750
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 5740-5750
    • Grauffel, C.1    Yang, B.2    He, T.3    Roberts, M.F.4    Gershenson, A.5    Reuter, N.6


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