메뉴 건너뛰기




Volumn 185, Issue 14, 2003, Pages 4081-4086

Determinants of the Src homology domain 3-like fold

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 0037816380     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.14.4081-4086.2003     Document Type: Article
Times cited : (21)

References (49)
  • 2
    • 0037180377 scopus 로고    scopus 로고
    • Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I from Synechocystis sp. PCC 6803
    • Barth, P., P. Savarin, B. Gilquin, B. Lagoutte, and F. Ochsenbein. 2002. Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I from Synechocystis sp. PCC 6803. Biochemistry 41:13902-13914.
    • (2002) Biochemistry , vol.41 , pp. 13902-13914
    • Barth, P.1    Savarin, P.2    Gilquin, B.3    Lagoutte, B.4    Ochsenbein, F.5
  • 3
    • 0033534368 scopus 로고    scopus 로고
    • Structure of CheA, a signal-transducing histidine kinase
    • Bilwes, A. M., L. A. Alex, B. R. Crane, and M. I. Simon. 1999. Structure of CheA, a signal-transducing histidine kinase. Cell 96:131-141.
    • (1999) Cell , vol.96 , pp. 131-141
    • Bilwes, A.M.1    Alex, L.A.2    Crane, B.R.3    Simon, M.I.4
  • 4
    • 0034307852 scopus 로고    scopus 로고
    • The iron dependent regulatory protein IdeR (DtxR) of Rhodococcus equi
    • Boland, C. A., and W. G. Meijer. 2000. The iron dependent regulatory protein IdeR (DtxR) of Rhodococcus equi. FEMS Microbiol. Lett. 191:1-5.
    • (2000) FEMS Microbiol. Lett. , vol.191 , pp. 1-5
    • Boland, C.A.1    Meijer, W.G.2
  • 5
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known 3-dimensional structure
    • Bowie, J. U., R. Luthy, and D. Eisenberg. 1991. A method to identify protein sequences that fold into a known 3-dimensional structure. Science 253:164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 6
    • 0024571640 scopus 로고
    • The helix-turn-helix DNA-binding morif
    • Brennan, R. G., and B. W. Matthews. 1989. The helix-turn-helix DNA-binding morif. J. Biol. Chem. 264:1903-1906.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1903-1906
    • Brennan, R.G.1    Matthews, B.W.2
  • 8
    • 0026743906 scopus 로고
    • Identification of a protein that binds to the Sh3 region of Abi and is similar to Bcr and Gap-Rho
    • Cicchetti, P., B. J. Mayer, G. Thiel, and D. Baltimore. 1992. Identification of a protein that binds to the Sh3 region of Abi and is similar to Bcr and Gap-Rho. Science 257:803-806.
    • (1992) Science , vol.257 , pp. 803-806
    • Cicchetti, P.1    Mayer, B.J.2    Thiel, G.3    Baltimore, D.4
  • 9
    • 0028895654 scopus 로고
    • Modular binding domains in signal-transduction proteins
    • Cohen, G. B., R. B. Ren, and D. Baltimore. 1995. Modular binding domains in signal-transduction proteins. Cell 80:237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.B.2    Baltimore, D.3
  • 10
    • 0029964556 scopus 로고    scopus 로고
    • Identification of the primary metal ion-activation sites of the diphtheria tox repressor by X-ray crystallography and site-directed mutational analysis
    • Ding, X., H. Zeng, N. Schiering, D. Ringe, and J. R. Murphy. 1996. Identification of the primary metal ion-activation sites of the diphtheria tox repressor by X-ray crystallography and site-directed mutational analysis. Nat. Struct. Biol. 3:382-387.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 382-387
    • Ding, X.1    Zeng, H.2    Schiering, N.3    Ringe, D.4    Murphy, J.R.5
  • 11
    • 0028198806 scopus 로고
    • 3-Dimensional solution structure of Psae from the Cyanobacterium synechococcus sp. strain Pcc-7002, a photosystem-I protein that shows structural homology with SH3 domains
    • Falzone, C. J., Y. H. Kao, J. D. Zhao, D. A. Bryant, and J. T. J. Lecomte. 1994. 3-Dimensional solution structure of Psae from the Cyanobacterium synechococcus sp. strain Pcc-7002, a photosystem-I protein that shows structural homology with SH3 domains. Biochemistry 33:6052-6062.
    • (1994) Biochemistry , vol.33 , pp. 6052-6062
    • Falzone, C.J.1    Kao, Y.H.2    Zhao, J.D.3    Bryant, D.A.4    Lecomte, J.T.J.5
  • 12
    • 0035937172 scopus 로고    scopus 로고
    • Crystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-angstrom resolution reveals the Src homology domain 3-like fold and metal binding function of the third domain
    • Feese, M. D., B. P. Ingason, J. Goranson-Siekierke, R. K. Holmes, and W. G. J. Hol. 2001. Crystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-angstrom resolution reveals the Src homology domain 3-like fold and metal binding function of the third domain. J. Biol. Chem. 276:5959-5966.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5959-5966
    • Feese, M.D.1    Ingason, B.P.2    Goranson-Siekierke, J.3    Holmes, R.K.4    Hol, W.G.J.5
  • 13
    • 0038243196 scopus 로고    scopus 로고
    • POVScript+: A program for model and data visualization using persistence of vision ray-tracing
    • Fenn, T. D., D. Ringe, and G. A. Petsko. 2003. POVScript+: a program for model and data visualization using persistence of vision ray-tracing. J. Appl. Crystallogr. 36:944-947.
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 944-947
    • Fenn, T.D.1    Ringe, D.2    Petsko, G.A.3
  • 14
    • 0027315204 scopus 로고
    • Characterization of an iron-regulated promoter involved in desferrioxamine B synthesis in Streptomyces pilosus: Repressor-binding site and homology to the diphtheria toxin gene promoter
    • Gunter, K., C. Toupet, and T. Schupp. 1993. Characterization of an iron-regulated promoter involved in desferrioxamine B synthesis in Streptomyces pilosus: repressor-binding site and homology to the diphtheria toxin gene promoter. J. Bacteriol. 175:3295-3302.
    • (1993) J. Bacteriol. , vol.175 , pp. 3295-3302
    • Gunter, K.1    Toupet, C.2    Schupp, T.3
  • 16
    • 84945096204 scopus 로고
    • Model bias in macromolecular crystal structures
    • Hodel, A., S. H. Kim, and A. T. Brunger. 1992. Model bias in macromolecular crystal structures. Acta Crystallogr. A 48:851-858.
    • (1992) Acta Crystallogr. A , vol.48 , pp. 851-858
    • Hodel, A.1    Kim, S.H.2    Brunger, A.T.3
  • 17
    • 0027440362 scopus 로고
    • Protein-struct ure comparison by alignment of distance matrices
    • Holm, L., and C. Sander. 1993. Protein-struct ure comparison by alignment of distance matrices. J. Mol. Biol. 233:123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 18
    • 0033815580 scopus 로고    scopus 로고
    • 2+) permease in Streptococcus gordonii is regulated by a diphtheria toxin metallorepressor-like protein ScaR
    • 2+) permease in Streptococcus gordonii is regulated by a diphtheria toxin metallorepressor-like protein ScaR. Mol. Microbiol. 38:140-153.
    • (2000) Mol. Microbiol. , vol.38 , pp. 140-153
    • Jakubovics, N.S.1    Smith, A.W.2    Jenkinson, H.F.3
  • 19
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones, T. A., J. Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47:110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 20
    • 0033081529 scopus 로고    scopus 로고
    • Rapid automated molecular replacement by evolutionary search
    • Kissinger, C. R., D. K. Gehlhaar, and D. B. Fogel. 1999. Rapid automated molecular replacement by evolutionary search. Acta Crystallogr. D 55:484-491.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 484-491
    • Kissinger, C.R.1    Gehlhaar, D.K.2    Fogel, D.B.3
  • 21
    • 0033943809 scopus 로고    scopus 로고
    • Genetic characterization of a Streptococcus mutans LraI family operon and its role in virulence
    • Kitten, T., C. L. Munro, S. M. Michalek, and F. L. Macrina. 2000. Genetic characterization of a Streptococcus mutans LraI family operon and its role in virulence. Infect. Immun. 68:4441-4451.
    • (2000) Infect. Immun. , vol.68 , pp. 4441-4451
    • Kitten, T.1    Munro, C.L.2    Michalek, S.M.3    Macrina, F.L.4
  • 22
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. 1991. Molscript - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0034486070 scopus 로고    scopus 로고
    • The identification of conserved interactions within the SH3 domain by alignment of sequences and structures
    • Larson, S. M., and A. R. Davidson. 2000. The identification of conserved interactions within the SH3 domain by alignment of sequences and structures, Protein Sci. 9:2170-2180.
    • (2000) Protein Sci. , vol.9 , pp. 2170-2180
    • Larson, S.M.1    Davidson, A.R.2
  • 24
    • 0000243829 scopus 로고
    • Procheck - A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. Macarthur, D. S. Moss, and J. M. Thornton. 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
  • 25
    • 0036845352 scopus 로고    scopus 로고
    • GW domains of the Listeria monocytogenes invasion protein InIB are SH3-like and mediate binding to host ligands
    • Marino, M., M. Banerjee, R. Jonquieres, P. Cossart, and P. Ghosh. 2002. GW domains of the Listeria monocytogenes invasion protein InIB are SH3-like and mediate binding to host ligands. EMBO J. 21:5623-5634.
    • (2002) EMBO J. , vol.21 , pp. 5623-5634
    • Marino, M.1    Banerjee, M.2    Jonquieres, R.3    Cossart, P.4    Ghosh, P.5
  • 26
    • 0033550071 scopus 로고    scopus 로고
    • The solution structure of photosystem I accessory protein E from the cyanobacterium Nostoc sp. strain PCC 8009
    • Mayer, K. L., G. Z. Shen, D. A. Bryant, J. T. J. Lecomte, and C. J. Falzone. 1999. The solution structure of photosystem I accessory protein E from the cyanobacterium Nostoc sp. strain PCC 8009. Biochemistry 38:13736-13746.
    • (1999) Biochemistry , vol.38 , pp. 13736-13746
    • Mayer, K.L.1    Shen, G.Z.2    Bryant, D.A.3    Lecomte, J.T.J.4    Falzone, C.J.5
  • 27
    • 0023723196 scopus 로고
    • Oligopeptide biases in protein sequences and their use in predicting protein coding regions in nucleotide sequences
    • McCaldon, P., and P. Argos. 1988. Oligopeptide biases in protein sequences and their use in predicting protein coding regions in nucleotide sequences. Proteins Struct. Funct. Genet. 4:99-122.
    • (1988) Proteins Struct. Funct. Genet. , vol.4 , pp. 99-122
    • McCaldon, P.1    Argos, P.2
  • 29
    • 0033559924 scopus 로고    scopus 로고
    • The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the fibosome
    • Nakagawa, A., T. Nakashima, M. Taniguchi, H. Hosaka, M. Kimura, and I. Tanaka. 1999. The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the fibosome. EMBO J. 18:1459-1467.
    • (1999) EMBO J. , vol.18 , pp. 1459-1467
    • Nakagawa, A.1    Nakashima, T.2    Taniguchi, M.3    Hosaka, H.4    Kimura, M.5    Tanaka, I.6
  • 30
    • 0028855065 scopus 로고
    • Molecular cloning, DNA sequence analysis, and characterization of the Corynebacterium diphtheriae Dtxr homolog from Brevibacterium lactofermentum
    • Oguiza, J. A., X. Tao, A. T. Marcos, M. Malumbres, J. F. Martin, and J. R. Murphy. 1995. Molecular cloning, DNA sequence analysis, and characterization of the Corynebacterium diphtheriae Dtxr homolog from Brevibacterium lactofermentum. J. Bacteriol. 177:465-467.
    • (1995) J. Bacteriol. , vol.177 , pp. 465-467
    • Oguiza, J.A.1    Tao, X.2    Marcos, A.T.3    Malumbres, M.4    Martin, J.F.5    Murphy, J.R.6
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0028859279 scopus 로고
    • Protein modules and signaling networks
    • Pawson, T. 1995. Protein modules and signaling networks. Nature 373:573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 33
    • 0000868851 scopus 로고    scopus 로고
    • Crystal structure of a cobalt-activated diphtheria toxin repressor-DNA complex reveals a metal-binding SH3-like domain
    • Pohl, E., R. K. Holmes, and W. G. J. Hol. 1999. Crystal structure of a cobalt-activated diphtheria toxin repressor-DNA complex reveals a metal-binding SH3-like domain. J. Mol. Biol. 292:653-667.
    • (1999) J. Mol. Biol. , vol.292 , pp. 653-667
    • Pohl, E.1    Holmes, R.K.2    Hol, W.G.J.3
  • 34
    • 0033057517 scopus 로고    scopus 로고
    • Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer
    • Ponting, C. P., L. Aravind, J. Schultz, P. Bork, and E. V. Koonin. 1999. Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer. J. Mol. Biol. 289:729-745.
    • (1999) J. Mol. Biol. , vol.289 , pp. 729-745
    • Ponting, C.P.1    Aravind, L.2    Schultz, J.3    Bork, P.4    Koonin, E.V.5
  • 35
    • 0032851843 scopus 로고    scopus 로고
    • Characterization of a manganese-dependent regulatory protein, TroR, from Treponema pallidum
    • Posey, J. E., J. M. Hardham, S. J. Norris, and F. C. Gherardini. 1999. Characterization of a manganese-dependent regulatory protein, TroR, from Treponema pallidum. Proc. Natl. Acad. Sci. USA 96:10887-10892.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10887-10892
    • Posey, J.E.1    Hardham, J.M.2    Norris, S.J.3    Gherardini, F.C.4
  • 36
    • 0029739483 scopus 로고    scopus 로고
    • High-resolution structure of the diphtheria toxin repressor complexed with cobalt and manganese reveals an SH3-like third domain and suggests a possible role of phosphate as co-corepressor
    • Qiu, X. Y., E. Pohl, R. K. Holmes, and W. G. J. Hol. 1996. High-resolution structure of the diphtheria toxin repressor complexed with cobalt and manganese reveals an SH3-like third domain and suggests a possible role of phosphate as co-corepressor. Biochemistry 35:12292-12302.
    • (1996) Biochemistry , vol.35 , pp. 12292-12302
    • Qiu, X.Y.1    Pohl, E.2    Holmes, R.K.3    Hol, W.G.J.4
  • 37
    • 0028993911 scopus 로고
    • 3-Dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors
    • Qiu, X. Y., C. Verlinde, S. P. Zhang, M. P. Schmitt, R. K. Holmes, and W. G. J. Hol. 1995.3-Dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors. Structure 3:87-100.
    • (1995) Structure , vol.3 , pp. 87-100
    • Qiu, X.Y.1    Verlinde, C.2    Zhang, S.P.3    Schmitt, M.P.4    Holmes, R.K.5    Hol, W.G.J.6
  • 38
    • 0033624818 scopus 로고    scopus 로고
    • Manganese homeostasis in Bacillus subtilis is regulated by MntR, a bifunctional regulator related to the diphtheria toxin repressor family of proteins
    • Que, Q., and J. D. Helmann. 2000. Manganese homeostasis in Bacillus subtilis is regulated by MntR, a bifunctional regulator related to the diphtheria toxin repressor family of proteins, Mol. Microbiol. 35:1454-1468.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1454-1468
    • Que, Q.1    Helmann, J.D.2
  • 40
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison - Assignment of global and residue confidence levels
    • Russell, R. B., and G. J. Barton. 1992. Multiple protein sequence alignment from tertiary structure comparison - assignment of global and residue confidence levels. Proteins Struct. Funct. Genet. 14:309-323.
    • (1992) Proteins Struct. Funct. Genet. , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 41
    • 0028971247 scopus 로고
    • Structural similarities in the noncatalytic domains of phenylalanyl transfer RNA and biotin synthetases
    • Safro, M., and L. Mosyak. 1995. Structural similarities in the noncatalytic domains of phenylalanyl transfer RNA and biotin synthetases. Protein Sci. 4:2429-2432.
    • (1995) Protein Sci. , vol.4 , pp. 2429-2432
    • Safro, M.1    Mosyak, L.2
  • 42
    • 0028826149 scopus 로고
    • Structures of the Apo-activated and the metal ion-activated forms of the diphtheria Tox repressor from Corynebacterium diphtheriae
    • Schiering, N., X. Tao, H. Y. Zeng, J. R. Murphy, G. A. Petsko, and D. Ringe. 1995. Structures of the Apo-activated and the metal ion-activated forms of the diphtheria Tox repressor from Corynebacterium diphtheriae. Proc. Natl. Acad. Sci. USA 92:9843-9850.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9843-9850
    • Schiering, N.1    Tao, X.2    Zeng, H.Y.3    Murphy, J.R.4    Petsko, G.A.5    Ringe, D.6
  • 43
    • 0027210121 scopus 로고
    • Analysis of diphtheria toxin repressor-operator interactions and characterization of a mutant repressor with decreased binding activity for divalent metals
    • Schmitt, M. P., and R. K. Holmes. 1993. Analysis of diphtheria toxin repressor-operator interactions and characterization of a mutant repressor with decreased binding activity for divalent metals. Mol. Microbiol. 9:173-181.
    • (1993) Mol. Microbiol. , vol.9 , pp. 173-181
    • Schmitt, M.P.1    Holmes, R.K.2
  • 44
    • 0028822995 scopus 로고
    • Characterization of an iron-dependent regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae
    • Schmitt, M. P., M. Predich, L. Doukhan, I. Smith, and R. K. Holmes. 1995. Characterization of an iron-dependent regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae. Infect. Immun. 63:4284-4289.
    • (1995) Infect. Immun. , vol.63 , pp. 4284-4289
    • Schmitt, M.P.1    Predich, M.2    Doukhan, L.3    Smith, I.4    Holmes, R.K.5
  • 45
    • 0033057129 scopus 로고    scopus 로고
    • Solution structure and peptide binding studies of the C-terminal Src homology 3-like domain of the diphtheria toxin repressor protein
    • Wang, G., G. P. Wylie, P. D. Twigg, D. L. D. Caspar, J. R. Murphy, and T. M. Logan. 1999. Solution structure and peptide binding studies of the C-terminal Src homology 3-like domain of the diphtheria toxin repressor protein. Proc. Natl. Acad. Sci. USA 96:6119-6124.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6119-6124
    • Wang, G.1    Wylie, G.P.2    Twigg, P.D.3    Caspar, D.L.D.4    Murphy, J.R.5    Logan, T.M.6
  • 47
    • 0032581662 scopus 로고    scopus 로고
    • Structure of the metal-ion-activated diphtheria toxin repressor tox operator complex
    • White, A., X. C. Ding, J. C. vanderSpek, J. R. Murphy, and D. Ringe. 1998. Structure of the metal-ion-activated diphtheria toxin repressor tox operator complex. Nature 394:502-506.
    • (1998) Nature , vol.394 , pp. 502-506
    • White, A.1    Ding, X.C.2    VanderSpek, J.C.3    Murphy, J.R.4    Ringe, D.5
  • 48
    • 0026666377 scopus 로고
    • Escherichia coli biotin holoenzyme synthetase biorepressor crystal structure delineates the biotin binding and DNA-binding domains
    • Wilson, K. P., L. M. Shewchuk, R. G. Brennan, A. J. Otsuka, and B. W. Matthews. 1992. Escherichia coli biotin holoenzyme synthetase biorepressor crystal structure delineates the biotin binding and DNA-binding domains. Proc. Natl. Acad. Sci. USA 89:9257-9261.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9257-9261
    • Wilson, K.P.1    Shewchuk, L.M.2    Brennan, R.G.3    Otsuka, A.J.4    Matthews, B.W.5
  • 49
    • 0027102571 scopus 로고
    • Solution structure of the Sh3 domain of Src and identification of its ligand-binding site
    • Yu, H. T., M. K. Rosen, T. B. Shin, C. Seideldugan, J. S. Brugge, and S. L. Schreiber. 1992. Solution structure of the Sh3 domain of Src and identification of its ligand-binding site. Science 258:1665-1668.
    • (1992) Science , vol.258 , pp. 1665-1668
    • Yu, H.T.1    Rosen, M.K.2    Shin, T.B.3    Seideldugan, C.4    Brugge, J.S.5    Schreiber, S.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.