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Volumn 18, Issue 7, 2011, Pages 907-919

The siderophore binding protein FeuA shows limited promiscuity toward exogenous triscatecholates

Author keywords

[No Author keywords available]

Indexed keywords

ENTEROCHELIN; FERRIC ION; OUTER MEMBRANE PROTEIN; SIDEROPHORE;

EID: 79960943873     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2011.05.006     Document Type: Article
Times cited : (35)

References (63)
  • 2
    • 69849115536 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of trilactone siderophores: Where chiral recognition occurs in enterobactin and bacillibactin iron transport
    • R.J. Abergel, A.M. Zawadzka, T.M. Hoette, and K.N. Raymond Enzymatic hydrolysis of trilactone siderophores: where chiral recognition occurs in enterobactin and bacillibactin iron transport J. Am. Chem. Soc. 131 2009 12682 12692
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 12682-12692
    • Abergel, R.J.1    Zawadzka, A.M.2    Hoette, T.M.3    Raymond, K.N.4
  • 5
    • 0037152372 scopus 로고    scopus 로고
    • Corynebactin and a serine trilactone based analogue: Chirality and molecular modeling of ferric complexes
    • M.E. Bluhm, B.P. Hay, S.S. Kim, E.A. Dertz, and K.N. Raymond Corynebactin and a serine trilactone based analogue: chirality and molecular modeling of ferric complexes Inorg. Chem. 41 2002 5475 5478
    • (2002) Inorg. Chem. , vol.41 , pp. 5475-5478
    • Bluhm, M.E.1    Hay, B.P.2    Kim, S.S.3    Dertz, E.A.4    Raymond, K.N.5
  • 6
  • 8
    • 0037010152 scopus 로고    scopus 로고
    • Iron transport and signaling in Escherichia coli
    • DOI 10.1016/S0014-5793(02)03185-X, PII S001457930203185X
    • V. Braun, and M. Braun Iron transport and signaling in Escherichia coli FEBS Lett. 529 2002 78 85 (Pubitemid 35283915)
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 78-85
    • Braun, V.1    Braun, M.2
  • 9
    • 34948822308 scopus 로고    scopus 로고
    • Docking of the periplasmic FecB binding protein to the FecCD transmembrane proteins in the ferric citrate transport system of Escherichia coli
    • DOI 10.1128/JB.00884-07
    • V. Braun, and C. Herrmann Docking of the periplasmic FecB binding protein to the FecCD transmembrane proteins in the ferric citrate transport system of Escherichia coli J. Bacteriol. 189 2007 6913 6918 (Pubitemid 47525435)
    • (2007) Journal of Bacteriology , vol.189 , Issue.19 , pp. 6913-6918
    • Braun, V.1    Herrmann, C.2
  • 10
    • 78650503779 scopus 로고    scopus 로고
    • Direct identification of a siderophore import protein using synthetic petrobactin ligands Angew. Chem. 122, 10408-10411
    • N. Bugdahn, F. Peuckert, A.G. Albrecht, M. Miethke, M.A. Marahiel, and M. Oberthur Direct identification of a siderophore import protein using synthetic petrobactin ligands Angew. Chem. 122, 10408-10411 Angew. Chem. Int. Ed. Engl. 49 2010 10210 10213
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 10210-10213
    • Bugdahn, N.1    Peuckert, F.2    Albrecht, A.G.3    Miethke, M.4    Marahiel, M.A.5    Oberthur, M.6
  • 11
    • 0018609981 scopus 로고
    • Ferric ion sequestering agents. II. Kinetics and mechanism of iron removal from transferrin by enterobactin and synthetic tricatechols
    • DOI 10.1021/ja00512a047
    • C.J. Carrano, and K.N. Raymond Ferric ion sequestering agents. 2. Kinetics and mechanism of iron removal from transferrin by enterobactin and synthetic tricatechols J. Am. Chem. Soc. 101 1979 5401 5404 (Pubitemid 10192379)
    • (1979) Journal of the American Chemical Society , vol.101 , Issue.18 , pp. 5401-5404
    • Carrano, C.J.1    Raymond, K.N.2
  • 12
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4
    • CCP4 The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 13
    • 34248634581 scopus 로고    scopus 로고
    • Molecular mechanism of ferricsiderophore passage through the outer membrane receptor proteins of Escherichia coli
    • DOI 10.1007/s10534-006-9060-9, Biometals: function and transport in bacteria, fungi, and humans
    • R. Chakraborty, E. Storey, and D. van der Helm Molecular mechanism of ferricsiderophore passage through the outer membrane receptor proteins of Escherichia coli Biometals 20 2007 263 274 (Pubitemid 46776574)
    • (2007) BioMetals , vol.20 , Issue.3-4 , pp. 263-274
    • Chakraborty, R.1    Storey, E.2    Van Der Helm, D.3
  • 14
    • 0033811814 scopus 로고    scopus 로고
    • Salicylic acid is not a bacterial siderophore: A theoretical study
    • J.R. Chipperfield, and C. Ratledge Salicylic acid is not a bacterial siderophore: a theoretical study Biometals 13 2000 165 168
    • (2000) Biometals , vol.13 , pp. 165-168
    • Chipperfield, J.R.1    Ratledge, C.2
  • 15
    • 0034127329 scopus 로고    scopus 로고
    • The structure of the ferric siderophore binding protein FhuD complexed with gallichrome
    • DOI 10.1038/74048
    • T.E. Clarke, S.Y. Ku, D.R. Dougan, H.J. Vogel, and L.W. Tari The structure of the ferric siderophore binding protein FhuD complexed with gallichrome Nat. Struct. Biol. 7 2000 287 291 (Pubitemid 30194451)
    • (2000) Nature Structural Biology , vol.7 , Issue.4 , pp. 287-291
    • Clarke, T.E.1    Ku, S.-Y.2    Dougan, D.R.3    Vogel, H.J.4    Tari, L.W.5
  • 16
    • 0037134502 scopus 로고    scopus 로고
    • X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin
    • DOI 10.1074/jbc.M109385200
    • T.E. Clarke, V. Braun, G. Winkelmann, L.W. Tari, and H.J. Vogel X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin J. Biol. Chem. 277 2002 13966 13972 (Pubitemid 34968004)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.16 , pp. 13966-13972
    • Clarke, T.E.1    Braun, V.2    Winkelmann, G.3    Tari, L.W.4    Vogel, H.J.5
  • 17
    • 0036260950 scopus 로고    scopus 로고
    • Ferric hydroxamate binding protein FhuD from Escherichia coli: Mutants in conserved and non-conserved regions
    • DOI 10.1023/A:1015249530156
    • T.E. Clarke, M.R. Rohrbach, L.W. Tari, H.J. Vogel, and W. Koster Ferric hydroxamate binding protein FhuD from Escherichia coli: mutants in conserved and non-conserved regions Biometals 15 2002 121 131 (Pubitemid 34494234)
    • (2002) BioMetals , vol.15 , Issue.2 , pp. 121-131
    • Clarke, T.E.1    Rohrbach, M.R.2    Tari, L.W.3    Vogel, H.J.4    Koster, W.5
  • 19
    • 0022528181 scopus 로고
    • Recognition and transport of ferric enterobactin in Escherichia coli
    • D.J. Ecker, B.F. Matzanke, and K.N. Raymond Recognition and transport of ferric enterobactin in Escherichia coli J. Bacteriol. 167 1986 666 673 (Pubitemid 16049987)
    • (1986) Journal of Bacteriology , vol.167 , Issue.2 , pp. 666-673
    • Ecker, D.J.1    Matzanke, B.F.2    Raymond, K.N.3
  • 22
    • 3242754298 scopus 로고    scopus 로고
    • Temperature control of a 3,4-dihydroxybenzoate (protocatechuate)-based siderophore in Bacillus anthracis
    • B.L. Garner, J.E. Arceneaux, and B.R. Byers Temperature control of a 3,4-dihydroxybenzoate (protocatechuate)-based siderophore in Bacillus anthracis Curr. Microbiol. 49 2004 89 94 (Pubitemid 38970712)
    • (2004) Current Microbiology , vol.49 , Issue.2 , pp. 89-94
    • Garner, B.L.1    Arceneaux, J.E.L.2    Byers, B.R.3
  • 24
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • DOI 10.1016/S1097-2765(02)00708-6
    • D.H. Goetz, M.A. Holmes, N. Borregaard, M.E. Bluhm, K.N. Raymond, and R.K. Strong The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition Mol. Cell 10 2002 1033 1043 (Pubitemid 36001971)
    • (2002) Molecular Cell , vol.10 , Issue.5 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5    Strong, R.K.6
  • 26
    • 77951234543 scopus 로고    scopus 로고
    • The Staphylococcus aureus siderophore receptor HtsA undergoes localized conformational changes to enclose staphyloferrin A in an arginine-rich binding pocket
    • J.C. Grigg, J.D. Cooper, J. Cheung, D.E. Heinrichs, and M.E. Murphy The Staphylococcus aureus siderophore receptor HtsA undergoes localized conformational changes to enclose staphyloferrin A in an arginine-rich binding pocket J. Biol. Chem. 285 2010 11162 11171
    • (2010) J. Biol. Chem. , vol.285 , pp. 11162-11171
    • Grigg, J.C.1    Cooper, J.D.2    Cheung, J.3    Heinrichs, D.E.4    Murphy, M.E.5
  • 27
    • 78049400552 scopus 로고    scopus 로고
    • Specificity of Staphyloferrin B recognition by the SirA receptor from Staphylococcus aureus
    • J.C. Grigg, J. Cheung, D.E. Heinrichs, and M.E. Murphy Specificity of Staphyloferrin B recognition by the SirA receptor from Staphylococcus aureus J. Biol. Chem. 285 2010 34579 34588
    • (2010) J. Biol. Chem. , vol.285 , pp. 34579-34588
    • Grigg, J.C.1    Cheung, J.2    Heinrichs, D.E.3    Murphy, M.E.4
  • 28
    • 0017691115 scopus 로고
    • Iron transport in Escherichia coli K 12. 2,3 Dihydroxybenzoate promoted iron uptake
    • DOI 10.1007/BF00446867
    • R.E. Hancock, K. Hantke, and V. Braun Iron transport in Escherichia coli K-12. 2,3-Dihydroxybenzoate-promoted iron uptake Arch. Microbiol. 114 1977 231 239 (Pubitemid 8183552)
    • (1977) Archives of Microbiology , vol.114 , Issue.3 , pp. 231-239
    • Hancock, R.E.W.1    Hantke, K.2    Braun, V.3
  • 29
    • 0035973739 scopus 로고    scopus 로고
    • Structural criteria for the rational design of selective ligands. 3. Quantitative structure-stability relationship for iron(III) complexation by tris-catecholamide siderophores
    • DOI 10.1021/ic001380s
    • B.P. Hay, D.A. Dixon, R. Vargas, J. Garza, and K.N. Raymond Structural criteria for the rational design of selective ligands. 3. Quantitative structure-stability relationship for iron(III) complexation by tris-catecholamide siderophores Inorg. Chem. 40 2001 3922 3935 (Pubitemid 32879681)
    • (2001) Inorganic Chemistry , vol.40 , Issue.16 , pp. 3922-3935
    • Hay, B.P.1    Dixon, D.A.2    Vargas, R.3    Garza, J.4    Raymond, K.N.5
  • 30
    • 11844301598 scopus 로고    scopus 로고
    • Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration
    • DOI 10.1016/j.str.2004.10.009, PII S0969212604003831
    • M.A. Holmes, W. Paulsene, X. Jide, C. Ratledge, and R.K. Strong Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration Structure 13 2005 29 41 (Pubitemid 40092472)
    • (2005) Structure , vol.13 , Issue.1 , pp. 29-41
    • Holmes, M.A.1    Paulsene, W.2    Jide, X.3    Ratledge, C.4    Strong, R.K.5
  • 31
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter - Binding protein complex BtuCD-BtuF
    • DOI 10.1126/science.1145950
    • R.N. Hvorup, B.A. Goetz, M. Niederer, K. Hollenstein, E. Perozo, and K.P. Locher Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF Science 317 2007 1387 1390 (Pubitemid 47417478)
    • (2007) Science , vol.317 , Issue.5843 , pp. 1387-1390
    • Hvorup, R.N.1    Goetz, B.A.2    Niederer, M.3    Hollenstein, K.4    Perozo, E.5    Locher, K.P.6
  • 33
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • W. Kabsch Integration, scaling, space-group assignment and post-refinement Acta Crystallogr. D Biol. Crystallogr. 66 2010 133 144
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 34
    • 33750736650 scopus 로고    scopus 로고
    • 12 binding protein BtuF
    • DOI 10.1021/bi061280j
    • 12 binding protein BtuF Biochemistry 45 2006 13284 13292 (Pubitemid 44707688)
    • (2006) Biochemistry , vol.45 , Issue.44 , pp. 13284-13292
    • Kandt, C.1    Xu, Z.2    Tieleman, D.P.3
  • 35
    • 0000563306 scopus 로고
    • Stereoselectivity in Chiral Fe(III) and Ga(III) Tris(Catecholate) complexes effected by nonbonded, weakly polar interactions
    • T.B. Karpishin, T.D.P. Stack, and K.N. Raymond Stereoselectivity in Chiral Fe(III) and Ga(III) Tris(Catecholate) complexes effected by nonbonded, weakly polar interactions J. Am. Chem. Soc. 115 1993 6115 6125
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 6115-6125
    • Karpishin, T.B.1    Stack, T.D.P.2    Raymond, K.N.3
  • 36
    • 0037424465 scopus 로고    scopus 로고
    • Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding
    • DOI 10.1074/jbc.M212239200
    • 12 suggest a functionally important reduction in protein mobility upon ligand binding J. Biol. Chem. 278 2003 8429 8434 (Pubitemid 36800593)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 8429-8434
    • Karpowich, N.K.1    Huang, H.H.2    Smith, P.C.3    Hunt, J.F.4
  • 37
    • 0034687759 scopus 로고    scopus 로고
    • Reconstitution and characterization of the Vibrio cholerae vibriobactin synthetase from VibB, VibE, VibF, and VibH
    • DOI 10.1021/bi0016523
    • T.A. Keating, C.G. Marshall, and C.T. Walsh Reconstitution and characterization of the Vibrio cholerae vibriobactin synthetase from VibB, VibE, VibF, and VibH Biochemistry 39 2000 15522 15530 (Pubitemid 32002779)
    • (2000) Biochemistry , vol.39 , Issue.50 , pp. 15522-15530
    • Keating, T.A.1    Marshall, C.G.2    Walsh, C.T.3
  • 38
    • 0030605248 scopus 로고    scopus 로고
    • A xylose-inducible Bacillus subtilis integration vector and its application
    • DOI 10.1016/S0378-1119(96)00466-0, PII S0378111996004660
    • L. Kim, A. Mogk, and W. Schumann A xylose-inducible Bacillus subtilis integration vector and its application Gene 181 1996 71 76 (Pubitemid 26418249)
    • (1996) Gene , vol.181 , Issue.1-2 , pp. 71-76
    • Kim, L.1    Mogk, A.2    Schumann, W.3
  • 40
    • 24744441871 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the periplasmic ferric-hydroxamate binding protein FhuD
    • DOI 10.1007/s10534-005-3712-z
    • K.D. Krewulak, C.M. Shepherd, and H.J. Vogel Molecular dynamics simulations of the periplasmic ferric-hydroxamate binding protein FhuD Biometals 18 2005 375 386 (Pubitemid 41298022)
    • (2005) BioMetals , vol.18 , Issue.4 , pp. 375-386
    • Krewulak, K.D.1    Shepherd, C.M.2    Vogel, H.J.3
  • 41
    • 50049089034 scopus 로고    scopus 로고
    • Structural biology of bacterial iron uptake
    • K.D. Krewulak, and H.J. Vogel Structural biology of bacterial iron uptake Biochim. Biophys. Acta 1778 2008 1781 1804
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1781-1804
    • Krewulak, K.D.1    Vogel, H.J.2
  • 42
    • 33751500166 scopus 로고
    • Solution equilibria of enterobactin and metal enterobactin complexes
    • L.D. Loomis, and K.N. Raymond Solution equilibria of enterobactin and metal enterobactin complexes Inorg. Chem. 30 1991 906 911
    • (1991) Inorg. Chem. , vol.30 , pp. 906-911
    • Loomis, L.D.1    Raymond, K.N.2
  • 43
    • 0022520145 scopus 로고
    • Escherichia coli iron enterobactin uptake monitored by Mossbauer spectroscopy
    • B.F. Matzanke, D.J. Ecker, T.S. Yang, B.H. Huynh, G. Muller, and K.N. Raymond Escherichia coli iron enterobactin uptake monitored by Mössbauer spectroscopy J. Bacteriol. 167 1986 674 680 (Pubitemid 16049988)
    • (1986) Journal of Bacteriology , vol.167 , Issue.2 , pp. 674-680
    • Matzanke, B.F.1    Ecker, D.J.2    Yang, T.-S.3
  • 44
    • 0035831486 scopus 로고    scopus 로고
    • The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin
    • J.J. May, T.M. Wendrich, and M.A. Marahiel The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin J. Biol. Chem. 276 2001 7209 7217
    • (2001) J. Biol. Chem. , vol.276 , pp. 7209-7217
    • May, J.J.1    Wendrich, T.M.2    Marahiel, M.A.3
  • 46
  • 47
    • 34548739613 scopus 로고    scopus 로고
    • Siderophore-based iron acquisition and pathogen control
    • DOI 10.1128/MMBR.00012-07
    • M. Miethke, and M.A. Marahiel Siderophore-based iron acquisition and pathogen control Microbiol. Mol. Biol. Rev. 71 2007 413 451 (Pubitemid 47429279)
    • (2007) Microbiology and Molecular Biology Reviews , vol.71 , Issue.3 , pp. 413-451
    • Miethke, M.1    Marahiel, M.A.2
  • 48
    • 77950157184 scopus 로고    scopus 로고
    • Neutrophil gelatinase-associated lipocalin expresses antimicrobial activity by interfering with l-norepinephrine-mediated bacterial iron acquisition
    • M. Miethke, and A. Skerra Neutrophil gelatinase-associated lipocalin expresses antimicrobial activity by interfering with l-norepinephrine-mediated bacterial iron acquisition Antimicrob. Agents Chemother. 54 2010 1580 1589
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 1580-1589
    • Miethke, M.1    Skerra, A.2
  • 51
    • 33646592214 scopus 로고    scopus 로고
    • Role of the Fur regulon in iron transport in Bacillus subtilis
    • DOI 10.1128/JB.188.10.3664-3673.2006
    • J. Ollinger, K.B. Song, H. Antelmann, M. Hecker, and J.D. Helmann Role of the Fur regulon in iron transport in Bacillus subtilis J. Bacteriol. 188 2006 3664 3673 (Pubitemid 43726229)
    • (2006) Journal of Bacteriology , vol.188 , Issue.10 , pp. 3664-3673
    • Ollinger, J.1    Song, K.-B.2    Antelmann, H.3    Hecker, M.4    Helmann, J.D.5
  • 52
    • 0014252383 scopus 로고
    • Itoic acid synthesis in Bacillus subtilis
    • W.J. Peters, and R.A. Warren Itoic acid synthesis in Bacillus subtilis J. Bacteriol. 95 1968 360 366
    • (1968) J. Bacteriol. , vol.95 , pp. 360-366
    • Peters, W.J.1    Warren, R.A.2
  • 53
    • 70349653359 scopus 로고    scopus 로고
    • Structural basis and stereochemistry of triscatecholate siderophore binding by FeuA. Angew. Chem. 121, 1040810411
    • F. Peuckert, M. Miethke, A.G. Albrecht, L.O. Essen, and M.A. Marahiel Structural basis and stereochemistry of triscatecholate siderophore binding by FeuA. Angew. Chem. 121, 1040810411 Angew. Chem. Int. Ed. Engl. 48 2009 7924 7927
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , pp. 7924-7927
    • Peuckert, F.1    Miethke, M.2    Albrecht, A.G.3    Essen, L.O.4    Marahiel, M.A.5
  • 54
    • 33845559030 scopus 로고
    • Coordination chemistry and microbial iron transport
    • K.N. Raymond, and C.J. Carrano Coordination chemistry and microbial iron transport Acc. Chem. Res. 12 1979 183 190
    • (1979) Acc. Chem. Res. , vol.12 , pp. 183-190
    • Raymond, K.N.1    Carrano, C.J.2
  • 57
    • 0346749526 scopus 로고    scopus 로고
    • The role of FhuD2 in iron(III)-hydroxamate transport in Staphylococcus aureus: Demonstration that FhuD2 binds iron(III)-hydroxamates but with minimal conformational change and implication of mutations on transport
    • DOI 10.1074/jbc.M305073200
    • M.T. Sebulsky, B.H. Shilton, C.D. Speziali, and D.E. Heinrichs The role of FhuD2 in iron(III)-hydroxamate transport in Staphylococcus aureus. Demonstration that FhuD2 binds iron(III)-hydroxamates but with minimal conformational change and implication of mutations on transport J. Biol. Chem. 278 2003 49890 49900 (Pubitemid 37548824)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 49890-49900
    • Sebulsky, M.T.1    Shilton, B.H.2    Speziali, C.D.3    Heinrichs, D.E.4
  • 58
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
    • A.J. Sharff, L.E. Rodseth, J.C. Spurlino, and F.A. Quiocho Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis Biochemistry 31 1992 10657 10663
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 59
    • 66149116873 scopus 로고    scopus 로고
    • Trapping open and closed forms of FitE: A group III periplasmic binding protein
    • R. Shi, A. Proteau, J. Wagner, Q. Cui, E.O. Purisima, A. Matte, and M. Cygler Trapping open and closed forms of FitE: a group III periplasmic binding protein Proteins 75 2009 598 609
    • (2009) Proteins , vol.75 , pp. 598-609
    • Shi, R.1    Proteau, A.2    Wagner, J.3    Cui, Q.4    Purisima, E.O.5    Matte, A.6    Cygler, M.7
  • 60
    • 0027524789 scopus 로고
    • Temporal activation of β-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool
    • J. Stülke, R. Hanschke, and M. Hecker Temporal activation of β-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool J. Gen. Microbiol. 139 1993 2041 2045 (Pubitemid 23284972)
    • (1993) Journal of General Microbiology , vol.139 , Issue.9 , pp. 2041-2045
    • Stulke, J.1    Hanschke, R.2    Hecker, M.3
  • 62
    • 3242891318 scopus 로고    scopus 로고
    • The DISOPRED server for the prediction of protein disorder
    • DOI 10.1093/bioinformatics/bth195
    • J.J. Ward, L.J. McGuffin, K. Bryson, B.F. Buxton, and D.T. Jones The Dros. Inf. Serv.OPRED server for the prediction of protein disorder Bioinformatics 20 2004 2138 2139 (Pubitemid 39236567)
    • (2004) Bioinformatics , vol.20 , Issue.13 , pp. 2138-2139
    • Ward, J.J.1    McGuffin, L.J.2    Bryson, K.3    Buxton, B.F.4    Jones, D.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.