메뉴 건너뛰기




Volumn 284, Issue 1, 1998, Pages 137-144

The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 Å resolution

Author keywords

Protein crystal structure; Serine protease structure; Subtilisin E; Subtilisin E propeptide complex; X ray crystallography

Indexed keywords

MUTANT PROTEIN; SUBTILISIN;

EID: 0032553556     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2161     Document Type: Article
Times cited : (149)

References (39)
  • 1
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement
    • Adams P. D., Pannu N. S., Read R. J., Brünger A. T. Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement. Proc. Natl Acad. Sci. USA. 94:1997;5018-5023.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5018-5023
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brünger, A.T.4
  • 2
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C. R. Principles that govern the folding of protein chains. Science. 181:1973;223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.R.1
  • 3
    • 0026605509 scopus 로고
    • A protein-folding reaction under kinetic control
    • Baker D., Sohl J. L., Agard D. A. A protein-folding reaction under kinetic control. Nature. 356:1992;263-265.
    • (1992) Nature , vol.356 , pp. 263-265
    • Baker, D.1    Sohl, J.L.2    Agard, D.A.3
  • 5
    • 0023643147 scopus 로고
    • The high-resolution X-ray crystal structure of the complex formed between subtilisin carlsberg and elgin c, an elastase inhibitor from the leech Hirudo medicinalis structural analysis, subtlisin structure and interface geometry
    • Bode W., Papamokos E., Musil D. The high-resolution X-ray crystal structure of the complex formed between subtilisin carlsberg and elgin c, an elastase inhibitor from the leech Hirudo medicinalis structural analysis, subtlisin structure and interface geometry. Eur. J. Biochem. 166:1987;673-692.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 673-692
    • Bode, W.1    Papamokos, E.2    Musil, D.3
  • 9
    • 0029645279 scopus 로고
    • Catalysis of a protein folding reaction: Mechanistic implications of the 2.0 Å structure of the subtilisin-prodomain complex
    • Bryan P., Wang L., Hoskins R., Strausberg S., Alexander P., Gilliland G., Gallagher T. Catalysis of a protein folding reaction: mechanistic implications of the 2.0 Å structure of the subtilisin-prodomain complex. Biochemistry. 34:1995;10310-10318.
    • (1995) Biochemistry , vol.34 , pp. 10310-10318
    • Bryan, P.1    Wang, L.2    Hoskins, R.3    Strausberg, S.4    Alexander, P.5    Gilliland, G.6    Gallagher, T.7
  • 11
    • 0029645412 scopus 로고
    • The prosegment-subtilisin BPN' complex: Crystal structure of a specific foldase
    • Gallagher T., Gilliland G., Wang L., Bryan P. The prosegment-subtilisin BPN' complex: crystal structure of a specific foldase. Structure. 3:1995;907-914.
    • (1995) Structure , vol.3 , pp. 907-914
    • Gallagher, T.1    Gilliland, G.2    Wang, L.3    Bryan, P.4
  • 12
    • 0023722280 scopus 로고
    • In vitro processing of pro-subtlisin produced in Escherichia coli
    • Ikemura H., Inouye M. In vitro processing of pro-subtlisin produced in Escherichia coli. J. Biol. Chem. 263:1988;12959-12963.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12959-12963
    • Ikemura, H.1    Inouye, M.2
  • 13
    • 0023644876 scopus 로고
    • Requirements of pro-sequence for the production of active subtilisin E in Escherichia coli
    • Ikemura H., Takagi H., Inouye M. Requirements of pro-sequence for the production of active subtilisin E in Escherichia coli. J. Biol. Chem. 262:1987;7859-7864.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7859-7864
    • Ikemura, H.1    Takagi, H.2    Inouye, M.3
  • 14
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 15
    • 0028067179 scopus 로고
    • Autoprocessing of pro-thiol-subtilisin E in which the active site serine residue 221 was altered to cystein
    • Li Y., Inouye M. Autoprocessing of pro-thiol-subtilisin E in which the active site serine residue 221 was altered to cystein. J. Biol. Chem. 269:1994;4169-4174.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4169-4174
    • Li, Y.1    Inouye, M.2
  • 16
    • 0028846035 scopus 로고
    • Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding: Purification and characterization of mutual propeptide
    • Li Y., Hu Z., Jordan F., Inouye M. Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding: purification and characterization of mutual propeptide. J. Biol. Chem. 270:1995;25127-25132.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25127-25132
    • Li, Y.1    Hu, Z.2    Jordan, F.3    Inouye, M.4
  • 18
    • 0039234462 scopus 로고
    • Subtilisins: Primary structure, chemical and physical properties
    • R.D. Boyer. New York: Academic Press
    • Markland F. S., Smith E. L. Subtilisins: primary structure, chemical and physical properties. Boyer R. D. The Enzymes. 1971;561-608 Academic Press, New York.
    • (1971) The Enzymes , pp. 561-608
    • Markland, F.S.1    Smith, E.L.2
  • 20
    • 0001851781 scopus 로고    scopus 로고
    • Application of maximum likelihood methods for macromolecular refinement
    • E. Dodson, M. Moore, A. Ralph, & S. Bailey. Warrington: CCLRC Daresbury Laboratory
    • Murshudov G., Dodson E., Vagin A. Application of maximum likelihood methods for macromolecular refinement. Dodson E., Moore M., Ralph A., Bailey S. Proceedings of the CCP4 Study Weekend: Macromolecular Refinement. 1996;93-104 CCLRC Daresbury Laboratory, Warrington.
    • (1996) Proceedings of the CCP4 Study Weekend: Macromolecular Refinement , pp. 93-104
    • Murshudov, G.1    Dodson, E.2    Vagin, A.3
  • 21
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 22
    • 84977282347 scopus 로고
    • Some uses of a best molecular fit routine
    • Nyburg S. C. Some uses of a best molecular fit routine. Acta Crystallog. sect. B. 30:1974;251-253.
    • (1974) Acta Crystallog. Sect. B , vol.30 , pp. 251-253
    • Nyburg, S.C.1
  • 23
    • 0027918137 scopus 로고
    • Alpha plus beta folds revisited: Some favoured motifs
    • Orengo C. A., Thornton J. M. Alpha plus beta folds revisited: some favoured motifs. Structure. 1:1993;105-120.
    • (1993) Structure , vol.1 , pp. 105-120
    • Orengo, C.A.1    Thornton, J.M.2
  • 24
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, & S. Bailey. Warrington: SERC Daresbury Laboratory
    • Otwinowski Z. Oscillation data reduction program. Sawyer L., Isaacs N., Bailey S. Proceedings of the CCP4 Study Weekend: Data Collection and Processing. 1993;56-62 SERC Daresbury Laboratory, Warrington.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 25
    • 0030809260 scopus 로고    scopus 로고
    • WARP: Improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic model
    • Perrakis A., Sixma T. K., Wilson K. S., Lamzin V. S. wARP: improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic model. Acta Crystallog. sect. D. 53:1997;448-455.
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 448-455
    • Perrakis, A.1    Sixma, T.K.2    Wilson, K.S.3    Lamzin, V.S.4
  • 26
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
    • Rice L. M., Brünger A. T. Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement. Proteins: Struct. Funct. Genet. 19:1994;277-290.
    • (1994) Proteins: Struct. Funct. Genet , vol.19 , pp. 277-290
    • Rice, L.M.1    Brünger, A.T.2
  • 27
    • 0000082544 scopus 로고
    • CHAIN - A crystallographic modeling program
    • Sack J. S. CHAIN - a crystallographic modeling program. J. Mol. Graph. 6:1988;224-225.
    • (1988) J. Mol. Graph. , vol.6 , pp. 224-225
    • Sack, J.S.1
  • 29
    • 0027421103 scopus 로고
    • Intramolecular chaperon & protein folding
    • Shinde U., Inouye M. Intramolecular chaperon & protein folding. Trends Biochem. Sci. 18:1993;442-446.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 442-446
    • Shinde, U.1    Inouye, M.2
  • 30
    • 0028949981 scopus 로고
    • Folding mediated by an intramolecular chaperone: Autoprocessing pathway of the precursor resolved via a substrate assisted catalysis mechanisim
    • Shinde U., Inouye M. Folding mediated by an intramolecular chaperone: autoprocessing pathway of the precursor resolved via a substrate assisted catalysis mechanisim. J. Mol. Biol. 247:1995a;390-395.
    • (1995) J. Mol. Biol. , vol.247 , pp. 390-395
    • Shinde, U.1    Inouye, M.2
  • 31
    • 0029123798 scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: Characterizationof the structural changes in pro-subtlisin E. coincident with autoprocessing
    • Shinde U., Inouye M. Folding pathway mediated by an intramolecular chaperone: characterizationof the structural changes in pro-subtlisin E. coincident with autoprocessing. J. Mol. Biol. 252:1995b;25-30.
    • (1995) J. Mol. Biol. , vol.252 , pp. 25-30
    • Shinde, U.1    Inouye, M.2
  • 32
    • 0024425004 scopus 로고
    • The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo
    • Silen J. L., Agard D. A. The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo. Nature. 341:1989;462-464.
    • (1989) Nature , vol.341 , pp. 462-464
    • Silen, J.L.1    Agard, D.A.2
  • 34
    • 0027244542 scopus 로고
    • Catalysis of a protein folding reaction: Thermodynamic and kinetic analysis of subtilisin BPN′ interactions with its propeptide fragment
    • Strausberg S., Alexander P., Wang L., Schwarz F., Bryan P. Catalysis of a protein folding reaction: thermodynamic and kinetic analysis of subtilisin BPN′ interactions with its propeptide fragment. Biochemistry. 32:1993;8112-8119.
    • (1993) Biochemistry , vol.32 , pp. 8112-8119
    • Strausberg, S.1    Alexander, P.2    Wang, L.3    Schwarz, F.4    Bryan, P.5
  • 36
    • 0025255159 scopus 로고
    • Unique precursor structure of an extracellular protease, aqualysin I, with NH2- and COOH-terminal pro-sequences and its processing in Escherichia coli
    • Terada I., Kwon S.-T., Miyata Y. Unique precursor structure of an extracellular protease, aqualysin I, with NH2- and COOH-terminal pro-sequences and its processing in Escherichia coli. J. Biol. Chem. 265:1990;6576-6581.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6576-6581
    • Terada, I.1    Kwon, S.-T.2    Miyata, Y.3
  • 37
    • 0026004831 scopus 로고
    • Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity
    • Winther J. R., Sorensen P. Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity. Proc. Natl Acad. Sci. USA. 88:1991;9330-9334.
    • (1991) Proc. Natl Acad. Sci. USA. , vol.88 , pp. 9330-9334
    • Winther, J.R.1    Sorensen, P.2
  • 38
    • 0022848673 scopus 로고
    • Determination of signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis
    • Wong S. L., Doi R. H. Determination of signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis. J. Biol. Chem. 261:1986;10176-10181.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10176-10181
    • Wong, S.L.1    Doi, R.H.2
  • 39
    • 0024409494 scopus 로고
    • Pro-sequence of subtilisin can guide the folding of denatured subtilisin in an intermolecular process
    • Zhu X., Ohta Y., Jordan F., Inouye M. Pro-sequence of subtilisin can guide the folding of denatured subtilisin in an intermolecular process. Nature. 339:1989;483-484.
    • (1989) Nature , vol.339 , pp. 483-484
    • Zhu, X.1    Ohta, Y.2    Jordan, F.3    Inouye, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.