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Volumn 5, Issue 6, 1997, Pages 813-824

The structure of Staphylococcus aureus epidermolytic toxin A, an atypic serine protease, at 1.7Å resolution

Author keywords

Epidermolytic toxin; Serine hydrolase; Serine protease; Staphylococcus aureus; X ray diffraction

Indexed keywords

ANIMALIA; BACTERIA (MICROORGANISMS); STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS;

EID: 12644258522     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00235-9     Document Type: Article
Times cited : (86)

References (69)
  • 1
    • 0014944960 scopus 로고
    • The staphylococcal scalded skin syndrome: Development of an experimental model
    • Melish, M.E. & Glasgow, L.A. (1970). The staphylococcal scalded skin syndrome: development of an experimental model. N. Engl. J. Med. 282, 1114-1119.
    • (1970) N. Engl. J. Med. , vol.282 , pp. 1114-1119
    • Melish, M.E.1    Glasgow, L.A.2
  • 2
    • 0015071651 scopus 로고
    • The staphylococcal scalded skin syndrome: The expanded clinical syndrome
    • Melish, M.E. & Glasgow, L.A. (1971). The staphylococcal scalded skin syndrome: the expanded clinical syndrome. J. Pediatr. 78, 958-967.
    • (1971) J. Pediatr. , vol.78 , pp. 958-967
    • Melish, M.E.1    Glasgow, L.A.2
  • 3
    • 0002099079 scopus 로고
    • Die exfoliative dermatitis jüngerer Säulinge
    • Ritter, V.R. (1878). Die exfoliative dermatitis jüngerer Säulinge. Cent. Z. Kinderheilkd. 2, 3-23.
    • (1878) Cent. Z. Kinderheilkd. , vol.2 , pp. 3-23
    • Ritter, V.R.1
  • 4
    • 0016747992 scopus 로고
    • Study of the mechanism of epidermal injury by a staphylococcal epidermolytic toxin
    • Wuepper, K.D., Dimond, R.L. & Knutson, D. (1975). Study of the mechanism of epidermal injury by a staphylococcal epidermolytic toxin. J. Invest. Dermatol. 65, 191-200.
    • (1975) J. Invest. Dermatol. , vol.65 , pp. 191-200
    • Wuepper, K.D.1    Dimond, R.L.2    Knutson, D.3
  • 5
    • 0013204459 scopus 로고
    • Two outbreaks of neonatal skin sepsis caused by Staphylococcus aureus
    • Howells, C.H.L. & Jones, E.H. (1961). Two outbreaks of neonatal skin sepsis caused by Staphylococcus aureus. Arch. Dis. Child. 36, 214-216.
    • (1961) Arch. Dis. Child. , vol.36 , pp. 214-216
    • Howells, C.H.L.1    Jones, E.H.2
  • 6
    • 0022631780 scopus 로고
    • Importance of exfoliatin toxin a production by Staphylococcus aureus strains isolated from clustered epidemics of neonatal pustulosis
    • Kaplan, M.H., Chmel, H., Hsieh, H.C., Stephens, A. & Brinsko, V. (1986). Importance of exfoliatin toxin A production by Staphylococcus aureus strains isolated from clustered epidemics of neonatal pustulosis. J. Clin. Microbiol. 23, 83-91.
    • (1986) J. Clin. Microbiol. , vol.23 , pp. 83-91
    • Kaplan, M.H.1    Chmel, H.2    Hsieh, H.C.3    Stephens, A.4    Brinsko, V.5
  • 7
    • 0023901253 scopus 로고
    • Staphylococcal scalded skin syndrome in two immunocompetent adults caused by exfoliatin B-producing Staphylococcus aureus
    • Opal, S.M., Johnson-Winegar, A.D. & Gross, A.S. (1988). Staphylococcal scalded skin syndrome in two immunocompetent adults caused by exfoliatin B-producing Staphylococcus aureus. J. Clin. Microbiol. 26, 1283-1286.
    • (1988) J. Clin. Microbiol. , vol.26 , pp. 1283-1286
    • Opal, S.M.1    Johnson-Winegar, A.D.2    Gross, A.S.3
  • 8
    • 0029970567 scopus 로고    scopus 로고
    • Staphylococcal scalded skin syndrome in an HIV-1 seropositive man
    • Farell, A.M., Ross, J.S., Unasankar, S. & Bunker, C.B. (1996). Staphylococcal scalded skin syndrome in an HIV-1 seropositive man. Brit. J. Dermatol. 134, 962-965.
    • (1996) Brit. J. Dermatol. , vol.134 , pp. 962-965
    • Farell, A.M.1    Ross, J.S.2    Unasankar, S.3    Bunker, C.B.4
  • 9
    • 0015107907 scopus 로고
    • Toxic epidermal necrolysis produced by an extracellular product of Staphylococcus aureus
    • Arbuthnott, J.P., Kent, J., Lyell, A. & Gemmell, C.G. (1971). Toxic epidermal necrolysis produced by an extracellular product of Staphylococcus aureus. Brit. J. Dermatol. 85, 145-149.
    • (1971) Brit. J. Dermatol. , vol.85 , pp. 145-149
    • Arbuthnott, J.P.1    Kent, J.2    Lyell, A.3    Gemmell, C.G.4
  • 10
    • 0015157796 scopus 로고
    • Product of Staphylococcus aureus responsible for the scalded-skin syndrome
    • Kapral, F.A. & Miller, M.M. (1971). Product of Staphylococcus aureus responsible for the scalded-skin syndrome, Infec. Immun. 4, 541-545.
    • (1971) Infec. Immun. , vol.4 , pp. 541-545
    • Kapral, F.A.1    Miller, M.M.2
  • 11
    • 0023203328 scopus 로고
    • Nucleotide sequence of the epidermolytic toxin a gene of Staphylococcus aureus
    • O'Toole, P.W. & Foster, T.J. (1987). Nucleotide sequence of the epidermolytic toxin A gene of Staphylococcus aureus. J. Bacteriol. 169, 3910-3915.
    • (1987) J. Bacteriol. , vol.169 , pp. 3910-3915
    • O'Toole, P.W.1    Foster, T.J.2
  • 12
    • 0023232764 scopus 로고
    • Sequence determination and comparison of the exfoliative toxin a and toxin B genes from Staphylococcus aureus
    • Lee, C.Y., Schmitt, J.J., Johnson, W.A.D., Spero, L. & landolo, J.J. (1987). Sequence determination and comparison of the exfoliative toxin A and toxin B genes from Staphylococcus aureus. J. Bacteriol. 169, 3904-3909.
    • (1987) J. Bacteriol. , vol.169 , pp. 3904-3909
    • Lee, C.Y.1    Schmitt, J.J.2    Johnson, W.A.D.3    Spero, L.4    Landolo, J.J.5
  • 13
    • 0021339430 scopus 로고
    • Epidemiological investigation of exfoliative toxin-producing Staphylococcus aureus strains in hospitalized patients
    • Piémont, Y., Rasoamananjara, D., Fouace, J.M. & Bruce, T. (1984). Epidemiological investigation of exfoliative toxin-producing Staphylococcus aureus strains in hospitalized patients. J. Clin. Microbiol. 19, 417-420.
    • (1984) J. Clin. Microbiol. , vol.19 , pp. 417-420
    • Piémont, Y.1    Rasoamananjara, D.2    Fouace, J.M.3    Bruce, T.4
  • 14
    • 0028016483 scopus 로고
    • A new type of staphylococcal exfoliative toxin from a Staphylococcus aureus strain isolated from a horse with phlegmon
    • Sato, H., Matsumori, Y., Tanabe, T., Saito, H., Shimizu, A. & Kawano, J. (1994). A new type of staphylococcal exfoliative toxin from a Staphylococcus aureus strain isolated from a horse with phlegmon. Infec. Immun. 62, 3780-3785.
    • (1994) Infec. Immun. , vol.62 , pp. 3780-3785
    • Sato, H.1    Matsumori, Y.2    Tanabe, T.3    Saito, H.4    Shimizu, A.5    Kawano, J.6
  • 15
    • 0025843651 scopus 로고
    • Isolation of exfoliative toxin from Staphylococcus hyicus and its exfoliative activity in the piglet
    • Sato, H., Tanabe, T., Kuramoto, M., Tanaka, K., Hashimoto, T. & Saito, H. (1991). Isolation of exfoliative toxin from Staphylococcus hyicus and its exfoliative activity in the piglet. Vet. Microbiol. 27, 263-275.
    • (1991) Vet. Microbiol. , vol.27 , pp. 263-275
    • Sato, H.1    Tanabe, T.2    Kuramoto, M.3    Tanaka, K.4    Hashimoto, T.5    Saito, H.6
  • 16
    • 0023634835 scopus 로고
    • Staphylococcal exfoliative toxin induces caseinolytic activity
    • Takiuchi, I., Kawamura, M., Teramoto, T. & Higuchi, D. (1987). Staphylococcal exfoliative toxin induces caseinolytic activity. J. Infec. Dis. 156, 508-509.
    • (1987) J. Infec. Dis. , vol.156 , pp. 508-509
    • Takiuchi, I.1    Kawamura, M.2    Teramoto, T.3    Higuchi, D.4
  • 17
    • 0026545492 scopus 로고
    • The esterolytic activity of epidermolytic toxins
    • 7. Bailey, C.J. & Redpath, M.B. (1992). The esterolytic activity of epidermolytic toxins. Biochem. J. 284, 177-180.
    • (1992) Biochem. J. , vol.284 , pp. 177-180
    • Bailey, C.J.1    Redpath, M.B.2
  • 19
    • 0025812454 scopus 로고
    • The role of the serine protease active site in the mode of action of epidermolytic toxin of Staphylococcus aureus
    • Redpath, M.B., Foster, T.J. & Bailey, C.J. (1991). The role of the serine protease active site in the mode of action of epidermolytic toxin of Staphylococcus aureus. FEMS Microbiol. Lett. 65, 151-155.
    • (1991) FEMS Microbiol. Lett. , vol.65 , pp. 151-155
    • Redpath, M.B.1    Foster, T.J.2    Bailey, C.J.3
  • 20
    • 0025900602 scopus 로고
    • Functional evidence that the Ser-195 residue of staphylococcal exfoliative toxin a is essential for biological activity
    • Prévost, G., Rifai, S., Chaix, M.L. & Piémont, Y. (1991). Functional evidence that the Ser-195 residue of staphylococcal exfoliative toxin A is essential for biological activity, Infec. Immun. 59, 3337-3339.
    • (1991) Infec. Immun. , vol.59 , pp. 3337-3339
    • Prévost, G.1    Rifai, S.2    Chaix, M.L.3    Piémont, Y.4
  • 21
    • 0026472409 scopus 로고
    • Secretory expression of a glutamic-acid-specific endopeptidase (Spase) from Staphylococcus aureus ATCC1 2600 in Bacillus subtilis
    • Kakudo, S., Yoshikawa, K., Tamaki, M., Nakamura, E. & Teraoka, H. (1992). Secretory expression of a glutamic-acid-specific endopeptidase (Spase) from Staphylococcus aureus ATCC1 2600 in Bacillus subtilis. Appl. Microbiol. Biotechnol. 38, 226-233.
    • (1992) Appl. Microbiol. Biotechnol. , vol.38 , pp. 226-233
    • Kakudo, S.1    Yoshikawa, K.2    Tamaki, M.3    Nakamura, E.4    Teraoka, H.5
  • 23
    • 0029972609 scopus 로고    scopus 로고
    • The superantigen exfoliative toxin induces cutaneous lymphocytes-associated antigen expression in peripheral human T lymphocytes
    • Zollner T.H., et al., & Kaufmann, R. (1996). The superantigen exfoliative toxin induces cutaneous lymphocytes-associated antigen expression in peripheral human T lymphocytes, Immunol. Lett. 49, 111-116.
    • (1996) Immunol. Lett. , vol.49 , pp. 111-116
    • Zollner, T.H.1    Kaufmann, R.2
  • 24
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A 42, 140-149.
    • (1986) Acta Cryst. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 25
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination. Applications of the free R value
    • Kleywegt, G.J. & Brünger, AT. (1996). Checking your imagination. Applications of the free R value. Structure 4, 897-904.
    • (1996) Structure , vol.4 , pp. 897-904
    • Kleywegt, G.J.1    Brünger, A.T.2
  • 26
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona, J.J. & Craik, C.S. (1995). Structural basis of substrate specificity in the serine proteases. Protein Sci. 4, 337-360.
    • (1995) Protein Sci. , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 27
    • 0029962944 scopus 로고    scopus 로고
    • Conservation and variability in the structures of serine proteinases of the chymotrypsin family
    • Lesk, A.M. & Fordham, W.D. (1996). Conservation and variability in the structures of serine proteinases of the chymotrypsin family. J. Mol. Biol. 258, 501-537.
    • (1996) J. Mol. Biol. , vol.258 , pp. 501-537
    • Lesk, A.M.1    Fordham, W.D.2
  • 28
    • 0023881841 scopus 로고
    • Refined crystal structure of Streptomyces griseus trypsin at 1.7Å resolution
    • Read, R.J. & James, M.N. (1988). Refined crystal structure of Streptomyces griseus trypsin at 1.7Å resolution. J. Mol. Biol. 200, 523-551.
    • (1988) J. Mol. Biol. , vol.200 , pp. 523-551
    • Read, R.J.1    James, M.N.2
  • 29
    • 0000441039 scopus 로고
    • Conformational substates and uncertainty in macromolecular free energy calculations
    • Model, A., Simonson, T., Fox, R.O. & Brünger, A.T. (1993). Conformational substates and uncertainty in macromolecular free energy calculations. J. Phys. Chem. 97, 3409-3417.
    • (1993) J. Phys. Chem. , vol.97 , pp. 3409-3417
    • Model, A.1    Simonson, T.2    Fox, R.O.3    Brünger, A.T.4
  • 30
    • 0029644248 scopus 로고
    • The catalytic site of serine proteinases as a specific binding cavity for xenon
    • Schiltz, M., Fourme, R., Broutin, I. & Prange, T. (1995). The catalytic site of serine proteinases as a specific binding cavity for xenon. Structured, 3, 309-316.
    • (1995) Structured , vol.3 , pp. 309-316
    • Schiltz, M.1    Fourme, R.2    Broutin, I.3    Prange, T.4
  • 31
    • 0025057072 scopus 로고
    • A serine protease triad forms the catalytic centre of a triaglycerol lipase
    • Brady, L., et al., & Menge, L.J. (1990). A serine protease triad forms the catalytic centre of a triaglycerol lipase. Nature 343, 767-770.
    • (1990) Nature , vol.343 , pp. 767-770
    • Brady, L.1    Menge, L.J.2
  • 32
    • 0025062291 scopus 로고
    • Structure of human pancreatic lipase
    • Winkler, F.K., D'Arcy, A. & Hunziker, W. (1990). Structure of human pancreatic lipase. Nature 343, 771-774.
    • (1990) Nature , vol.343 , pp. 771-774
    • Winkler, F.K.1    D'Arcy, A.2    Hunziker, W.3
  • 33
    • 0026418174 scopus 로고
    • A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex
    • Brzozowski, A.M., et al., & Thim, L. (1991). A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature 351, 491-494.
    • (1991) Nature , vol.351 , pp. 491-494
    • Brzozowski, A.M.1    Thim, L.2
  • 34
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I. & Berger, A. (1967). On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 35
    • 0029901182 scopus 로고    scopus 로고
    • Novel features of serine protease active sites and specificity pockets: Sequence analysis and modelling studies of glutamate-specific endopeptidases and epidermolytic toxins
    • Barbosa, J.A., Saldanha, J.W. & Garatt, R.C. (1996). Novel features of serine protease active sites and specificity pockets: sequence analysis and modelling studies of glutamate-specific endopeptidases and epidermolytic toxins. Protein Eng. 9, 591-601.
    • (1996) Protein Eng. , vol.9 , pp. 591-601
    • Barbosa, J.A.1    Saldanha, J.W.2    Garatt, R.C.3
  • 36
    • 0027486963 scopus 로고
    • A glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding
    • Nienaber, V.L., Breddam, K. & Birktoft, J.J. (1993). A glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding. Biochemistry 32, 11469-11475.
    • (1993) Biochemistry , vol.32 , pp. 11469-11475
    • Nienaber, V.L.1    Breddam, K.2    Birktoft, J.J.3
  • 37
    • 0029658225 scopus 로고    scopus 로고
    • Characterization of the S1 binding site of the glutamic acid-specific protease from Streptomycesgriseus
    • Stennicke, H.R., Birkhoft, J.J. & Breddam, K. (1996). Characterization of the S1 binding site of the glutamic acid-specific protease from Streptomycesgriseus. Protein Sci. 5, 2266-2275.
    • (1996) Protein Sci. , vol.5 , pp. 2266-2275
    • Stennicke, H.R.1    Birkhoft, J.J.2    Breddam, K.3
  • 38
    • 0026503259 scopus 로고
    • Substrates preferences of glutamic acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching
    • Breddam, K. & Meldam, M. (1992). Substrates preferences of glutamic acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching. Eur. J. Biochem. 206, 103-107.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 103-107
    • Breddam, K.1    Meldam, M.2
  • 39
    • 0025119636 scopus 로고
    • Action of staphylococcal exfoliative toxins on epidermal cell cultures and organotropic skin
    • Gentilhomme, E., Faure, M., Piémont, Y., Binder, P. & Thivolet, J. (1990). Action of staphylococcal exfoliative toxins on epidermal cell cultures and organotropic skin. J. Dermatol. 17, 526-532.
    • (1990) J. Dermatol. , vol.17 , pp. 526-532
    • Gentilhomme, E.1    Faure, M.2    Piémont, Y.3    Binder, P.4    Thivolet, J.5
  • 40
    • 0025367679 scopus 로고
    • The staphylococcal enterotoxins and their relatives
    • Marrack, P. & Kappler, J.W. (1990). The staphylococcal enterotoxins and their relatives. Science 248, 705-711.
    • (1990) Science , vol.248 , pp. 705-711
    • Marrack, P.1    Kappler, J.W.2
  • 41
    • 0026512972 scopus 로고
    • Recombinant epidermolytic (exfoliative) toxin a of Staphylococcus aureus is not a superantigen
    • Fleischer, B. & Bailey, C.J. (1992). Recombinant epidermolytic (exfoliative) toxin A of Staphylococcus aureus is not a superantigen. Med. Microbiol. Immunol. 180, 273-278.
    • (1992) Med. Microbiol. Immunol. , vol.180 , pp. 273-278
    • Fleischer, B.1    Bailey, C.J.2
  • 42
    • 0029840436 scopus 로고    scopus 로고
    • Treatment of intracranial tumors by systemic transfer of superantigen-activated tumor-draining lymph node T cells
    • Inoue, M., Plantz, G.E. & Shu, S. (1996). Treatment of intracranial tumors by systemic transfer of superantigen-activated tumor-draining lymph node T cells. Cancer Res. 56, 4702-4708.
    • (1996) Cancer Res. , vol.56 , pp. 4702-4708
    • Inoue, M.1    Plantz, G.E.2    Shu, S.3
  • 43
    • 0028914523 scopus 로고
    • Identification and purification of a new staphylococcal enterotoxin, H
    • Su, Y.-C. & Wong, A.C.L. (1995). Identification and purification of a new staphylococcal enterotoxin, H. Appl. Environ. Microbiol. 61, 1438-1443.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1438-1443
    • Su, Y.-C.1    Wong, A.C.L.2
  • 44
    • 0017263168 scopus 로고
    • Preparation of chromophoric substrates for the glutamoyl specific staphylococcal protease
    • Houmard, J. (1976). Preparation of chromophoric substrates for the glutamoyl specific staphylococcal protease. Int. J. Pept. Protein Res. 8, 199-204.
    • (1976) Int. J. Pept. Protein Res. , vol.8 , pp. 199-204
    • Houmard, J.1
  • 45
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J. & Messing, J. (1985). Improved M13 phage cloning vectors and host strains: nucleotide sequences of M13mp18 and pUC19 vectors. Gene 33, 103-109.
    • (1985) Gene , vol.33 , pp. 103-109
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 46
    • 0343096316 scopus 로고
    • DNA sequence analysis with a modified bacteriophage T7 polymerase
    • Tabor, S. & Richardson, C.C. (1987). DNA sequence analysis with a modified bacteriophage T7 polymerase. Proc. Natl. Acad. Sci. USA. 77, 4761-4771.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4761-4771
    • Tabor, S.1    Richardson, C.C.2
  • 47
    • 0025079412 scopus 로고
    • Transformation of Staphylococcus epidermidis and other staphylococcal species with plasmid DNA electroporation
    • Augustin, J. & Götz, F. (1990). Transformation of Staphylococcus epidermidis and other staphylococcal species with plasmid DNA electroporation. FEMS Microbiol. Lett. 54, 203-207.
    • (1990) FEMS Microbiol. Lett. , vol.54 , pp. 203-207
    • Augustin, J.1    Götz, F.2
  • 48
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. (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
  • 49
    • 85046526624 scopus 로고
    • Evaluation of single crystal X-ray diffraction data from a position sensitive detector
    • Kabsch, W. (1988). Evaluation of single crystal X-ray diffraction data from a position sensitive detector. J. Appl. Cryst. 21, 916-924.
    • (1988) J. Appl. Cryst. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 50
    • 0028103275 scopus 로고
    • The CCP4 suite : Programs for protein crystallography
    • Collaborative Computational Project No. 4. (1994). The CCP4 suite : programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 51
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavyatom parameter refinement in the MIR and MAD methods
    • De La Fortelle, E. & Bricogne, G. (1997). Maximum-likelihood heavyatom parameter refinement in the MIR and MAD methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 52
    • 0000449646 scopus 로고
    • Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints
    • Cowtan, K.D. & Main, P. (1993). Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints. Acta Cryst. D 49, 148-157.
    • (1993) Acta Cryst. D , vol.49 , pp. 148-157
    • Cowtan, K.D.1    Main, P.2
  • 53
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J.P. & Leslie, G.W. (1996). Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Cryst. D 52, 30-42.
    • (1996) Acta Cryst. D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, G.W.2
  • 54
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cown, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cown, S.W.3    Kjeldgaard, M.4
  • 56
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 57
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 335, 472-474.
    • (1992) Nature , vol.335 , pp. 472-474
    • Brünger, A.T.1
  • 58
    • 0028774713 scopus 로고
    • Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid
    • Kleywegt, G.J. & Jones, T.A. (1994). Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid. Structure 2, 1241-1258.
    • (1994) Structure , vol.2 , pp. 1241-1258
    • Kleywegt, G.J.1    Jones, T.A.2
  • 59
    • 0030497978 scopus 로고    scopus 로고
    • Efficient rebuilding of protein structures
    • Kleywegt, G.J. & Jones, T.A. (1996). Efficient rebuilding of protein structures. Acta Cryst. D52, 829-832.
    • (1996) Acta Cryst. D , vol.52 , pp. 829-832
    • Kleywegt, G.J.1    Jones, T.A.2
  • 60
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskwoski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskwoski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 61
    • 0025398721 scopus 로고
    • WHATIF: A molecular modelling and drug design program
    • Vriend, G. (1990). WHATIF: a molecular modelling and drug design program. J. Mol. Graphics 8, 52-56.
    • (1990) J. Mol. Graphics , vol.8 , pp. 52-56
    • Vriend, G.1
  • 62
    • 0027542118 scopus 로고
    • Quality control of protein models : Directional atomic contact analysis
    • Vriend, G. & Sander, C. (1993). Quality control of protein models : directional atomic contact analysis. J. Appl. Cryst. 26, 47-60.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 47-60
    • Vriend, G.1    Sander, C.2
  • 64
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. (1993). SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics 11, 134-138.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 65
    • 0022405087 scopus 로고
    • Electron density calculations as an extension of protein structure refinement. Streptomyces griseus protease at 1.5A resolution
    • Moult, J., Sussman, F. & James, M.N. (1985). Electron density calculations as an extension of protein structure refinement. Streptomyces griseus protease at 1.5A resolution. J. Mol. Biol. 182, 555-566.
    • (1985) J. Mol. Biol. , vol.182 , pp. 555-566
    • Moult, J.1    Sussman, F.2    James, M.N.3
  • 66
    • 0021102433 scopus 로고
    • Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8Å resolution
    • Read, R.J., Fujinaga, M., Sielecki, A.R. & James, M.N. (1983). Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8Å resolution. Biochemistry 22, 4420-4433.
    • (1983) Biochemistry , vol.22 , pp. 4420-4433
    • Read, R.J.1    Fujinaga, M.2    Sielecki, A.R.3    James, M.N.4
  • 67
    • 0021881957 scopus 로고
    • Refined structure of alpha-lytic protease at 1.7Å resolution. Analysis of hydrogen bonding and solvent structure
    • Fujinaga, M., Delbaere, L.T., Brayer, G.D. & James, M.N. (1985). Refined structure of alpha-lytic protease at 1.7Å resolution. Analysis of hydrogen bonding and solvent structure. J. Mol. Biol. 184, 479-502.
    • (1985) J. Mol. Biol. , vol.184 , pp. 479-502
    • Fujinaga, M.1    Delbaere, L.T.2    Brayer, G.D.3    James, M.N.4
  • 68
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF: A program to identify and analyze structural motifs in proteins
    • Hutchinson, E.G. & Thornton, J.M. (1996). PROMOTIF: A program to identify and analyze structural motifs in proteins. Protein Sci. 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 69
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.