메뉴 건너뛰기




Volumn 400, Issue 4, 2010, Pages 865-877

Crystal structure of a subtilisin homologue, Tk-SP, from thermococcus kodakaraensis: Requirement of a C-terminal β-Jelly Roll domain for hyperstability

Author keywords

Crystal structure; Hyperthermophilic archaeon; Jelly roll domain; Serine protease; Thermococcus kodakaraensis

Indexed keywords

CALCIUM ION; EDETIC ACID; SERINE PROTEINASE; SERINE PROTEINASE TK SP; SUBTILISIN; UNCLASSIFIED DRUG;

EID: 77954385453     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.05.064     Document Type: Article
Times cited : (38)

References (57)
  • 1
    • 0029543755 scopus 로고    scopus 로고
    • Propeptide-mediated folding in subtilisin: the intramolecular chaperone concept
    • Shinde U., Inouye M. Propeptide-mediated folding in subtilisin: the intramolecular chaperone concept. Adv. Exp. Med. Biol. 1996, 379:147-154.
    • (1996) Adv. Exp. Med. Biol. , vol.379 , pp. 147-154
    • Shinde, U.1    Inouye, M.2
  • 2
    • 0027451307 scopus 로고
    • Folding of subtilisin BPN': role of the pro-sequence
    • Eder J., Rheinnecker M., Fersht A.R. Folding of subtilisin BPN': role of the pro-sequence. J. Mol. Biol. 1993, 233:293-304.
    • (1993) J. Mol. Biol. , vol.233 , pp. 293-304
    • Eder, J.1    Rheinnecker, M.2    Fersht, A.R.3
  • 3
    • 0028973036 scopus 로고
    • Prodomain mutations at the subtilisin interface: correlation of binding energy and the rate of catalyzed folding
    • Wang L., Ruvinov S., Strausberg S., Gallagher T., Gilliland G.L., Bryan P.N. Prodomain mutations at the subtilisin interface: correlation of binding energy and the rate of catalyzed folding. Biochemistry 1995, 34:15415-15420.
    • (1995) Biochemistry , vol.34 , pp. 15415-15420
    • Wang, L.1    Ruvinov, S.2    Strausberg, S.3    Gallagher, T.4    Gilliland, G.L.5    Bryan, P.N.6
  • 4
    • 0032478201 scopus 로고    scopus 로고
    • Engineering the independent folding of the subtilisin BPN'-pro-domain: correlation of pro-domain stability with the rate of subtilisin folding
    • Wang L., Ruan B., Ruvinov S., Bryan P.N. Engineering the independent folding of the subtilisin BPN'-pro-domain: correlation of pro-domain stability with the rate of subtilisin folding. Biochemistry 1998, 37:3165-3171.
    • (1998) Biochemistry , vol.37 , pp. 3165-3171
    • Wang, L.1    Ruan, B.2    Ruvinov, S.3    Bryan, P.N.4
  • 5
    • 0034490227 scopus 로고    scopus 로고
    • Intramolecular chaperones: polypeptide extensions that modulate protein folding
    • Shinde U.P., Inouye M. Intramolecular chaperones: polypeptide extensions that modulate protein folding. Semin. Cell Dev. Biol. 2000, 11:35-44.
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 35-44
    • Shinde, U.P.1    Inouye, M.2
  • 6
    • 0034596066 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone. The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked
    • Fu X., Inouye M., Shinde U.P. Folding pathway mediated by an intramolecular chaperone. The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked. J. Biol. Chem. 2000, 275:16871-16878.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16871-16878
    • Fu, X.1    Inouye, M.2    Shinde, U.P.3
  • 7
    • 0035976917 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin
    • Yabuta Y., Takagi H., Inouye M., Shinde U.P. Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin. J. Biol. Chem. 2001, 276:44427-44443.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44427-44443
    • Yabuta, Y.1    Takagi, H.2    Inouye, M.3    Shinde, U.P.4
  • 8
    • 0037674588 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone. A functional peptide chaperone designed using sequence databases
    • Yabuta Y., Subbian E., Oiry C., Shinde U.P. Folding pathway mediated by an intramolecular chaperone. A functional peptide chaperone designed using sequence databases. J. Biol. Chem. 2003, 278:15246-15251.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15246-15251
    • Yabuta, Y.1    Subbian, E.2    Oiry, C.3    Shinde, U.P.4
  • 9
    • 14644437656 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: intrinsically unstructured propeptide modulates stochastic activation of subtilisin
    • Subbian E., Yabuta Y., Shinde U.P. Folding pathway mediated by an intramolecular chaperone: intrinsically unstructured propeptide modulates stochastic activation of subtilisin. J. Mol. Biol. 2005, 347:367-383.
    • (2005) J. Mol. Biol. , vol.347 , pp. 367-383
    • Subbian, E.1    Yabuta, Y.2    Shinde, U.P.3
  • 10
    • 33846400026 scopus 로고    scopus 로고
    • Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E.
    • Falzon L., Patel S., Chen Y.J., Inouye M. Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E. J. Mol. Biol. 2007, 366:494-503.
    • (2007) J. Mol. Biol. , vol.366 , pp. 494-503
    • Falzon, L.1    Patel, S.2    Chen, Y.J.3    Inouye, M.4
  • 12
    • 0030896832 scopus 로고    scopus 로고
    • Subtilases: the superfamily of subtilisin-like serine proteases
    • Siezen R.J., Leunissen J.A. Subtilases: the superfamily of subtilisin-like serine proteases. Protein Sci. 1997, 6:501-523.
    • (1997) Protein Sci. , vol.6 , pp. 501-523
    • Siezen, R.J.1    Leunissen, J.A.2
  • 13
    • 0024817865 scopus 로고
    • Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 Å resolution and comparison of two crystal forms that differ in calcium content
    • Gros P., Betzel C., Dauter Z., Wilson K.S., Hol W.G. Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 Å resolution and comparison of two crystal forms that differ in calcium content. J. Mol. Biol. 1988, 210:347-367.
    • (1988) J. Mol. Biol. , vol.210 , pp. 347-367
    • Gros, P.1    Betzel, C.2    Dauter, Z.3    Wilson, K.S.4    Hol, W.G.5
  • 14
    • 0024191755 scopus 로고
    • Three-dimensional structure of proteinase K at 0.15-nm resolution
    • Betzel C., Pal G.P., Saenger W. Three-dimensional structure of proteinase K at 0.15-nm resolution. Eur. J. Biochem. 1988, 178:155-171.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 155-171
    • Betzel, C.1    Pal, G.P.2    Saenger, W.3
  • 15
    • 0023729499 scopus 로고
    • Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo
    • McPhalen C.A., James M.N. Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo. Biochemistry 1988, 27:6582-6598.
    • (1988) Biochemistry , vol.27 , pp. 6582-6598
    • McPhalen, C.A.1    James, M.N.2
  • 18
    • 0017075046 scopus 로고
    • Role of bound calcium ions in thermostable, proteolytic enzymes. Separation of intrinsic and calcium ion contributions to the kinetic thermal stability
    • Voordouw G., Milo C., Roche R.S. Role of bound calcium ions in thermostable, proteolytic enzymes. Separation of intrinsic and calcium ion contributions to the kinetic thermal stability. Biochemistry 1976, 15:3716-3724.
    • (1976) Biochemistry , vol.15 , pp. 3716-3724
    • Voordouw, G.1    Milo, C.2    Roche, R.S.3
  • 19
    • 0024962392 scopus 로고
    • Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding
    • Pantoliano M.W., Whitlow M., Wood J.F., Dodd S.W., Hardman K.D., Rollence M.L., Bryan P.N. Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding. Biochemistry 1989, 28:7205-7213.
    • (1989) Biochemistry , vol.28 , pp. 7205-7213
    • Pantoliano, M.W.1    Whitlow, M.2    Wood, J.F.3    Dodd, S.W.4    Hardman, K.D.5    Rollence, M.L.6    Bryan, P.N.7
  • 20
    • 0024959484 scopus 로고
    • Long-range structural changes in proteinase K triggered by calcium ion removal
    • Bajorath J., Raghunathan S., Hinrichs W., Saenger W. Long-range structural changes in proteinase K triggered by calcium ion removal. Nature 1989, 337:481-484.
    • (1989) Nature , vol.337 , pp. 481-484
    • Bajorath, J.1    Raghunathan, S.2    Hinrichs, W.3    Saenger, W.4
  • 22
    • 13544250517 scopus 로고    scopus 로고
    • Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes
    • Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T. Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes. Genome Res. 2005, 15:352-363.
    • (2005) Genome Res. , vol.15 , pp. 352-363
    • Fukui, T.1    Atomi, H.2    Kanai, T.3    Matsumi, R.4    Fujiwara, S.5    Imanaka, T.6
  • 23
    • 0035379692 scopus 로고    scopus 로고
    • Active subtilisin-like protease from a hyperthermophilic archaeon in a form with a putative prosequence
    • Kannan Y., Koga Y., Inoue Y., Haruki M., Takagi M., Imanaka T., et al. Active subtilisin-like protease from a hyperthermophilic archaeon in a form with a putative prosequence. Appl. Environ. Microbiol. 2001, 67:2445-2452.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2445-2452
    • Kannan, Y.1    Koga, Y.2    Inoue, Y.3    Haruki, M.4    Takagi, M.5    Imanaka, T.6
  • 24
    • 33745182284 scopus 로고    scopus 로고
    • 2+-dependent maturation of Tk-subtilisin from a hyperthermophilic archaeon: propeptide is a potent inhibitor of the mature domain but is not required for its folding
    • 2+-dependent maturation of Tk-subtilisin from a hyperthermophilic archaeon: propeptide is a potent inhibitor of the mature domain but is not required for its folding. Appl. Environ. Microbiol. 2006, 72:4154-4162.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 4154-4162
    • Pulido, M.1    Saito, K.2    Tanaka, S.3    Koga, Y.4    Morikawa, M.5    Takano, K.6    Kanaya, S.7
  • 25
    • 33748481991 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction study of active-site mutant of Pro-Tk-subtilisin from a hyperthermophilic archaeon
    • Tanaka S., Saita K., Chon H., Matsumura H., Koga Y., Takano K., Kanaya S. Crystallization and preliminary X-ray diffraction study of active-site mutant of Pro-Tk-subtilisin from a hyperthermophilic archaeon. Acta Crystallogr., Sect. F 2006, 62:902-905.
    • (2006) Acta Crystallogr., Sect. F , vol.62 , pp. 902-905
    • Tanaka, S.1    Saita, K.2    Chon, H.3    Matsumura, H.4    Koga, Y.5    Takano, K.6    Kanaya, S.7
  • 26
    • 34047216653 scopus 로고    scopus 로고
    • Directed evolution of Tk-subtilisin from a hyperthermophilic archaeon: identification of a single amino acid substitution in the propeptide region responsible for low-temperature adaptation
    • Pulido M., Koga Y., Takano K., Kanaya S. Directed evolution of Tk-subtilisin from a hyperthermophilic archaeon: identification of a single amino acid substitution in the propeptide region responsible for low-temperature adaptation. Protein Eng. Des. Sel. 2007, 20:143-153.
    • (2007) Protein Eng. Des. Sel. , vol.20 , pp. 143-153
    • Pulido, M.1    Koga, Y.2    Takano, K.3    Kanaya, S.4
  • 27
    • 34548394557 scopus 로고    scopus 로고
    • Four new crystal structures of Tk-subtilisin in unautoprocessed, autoprocessed and mature forms: insight into structural changes during maturation
    • Tanaka S., Matsumura H., Koga Y., Takano K., Kanaya S. Four new crystal structures of Tk-subtilisin in unautoprocessed, autoprocessed and mature forms: insight into structural changes during maturation. J. Mol. Biol. 2007, 372:1055-1069.
    • (2007) J. Mol. Biol. , vol.372 , pp. 1055-1069
    • Tanaka, S.1    Matsumura, H.2    Koga, Y.3    Takano, K.4    Kanaya, S.5
  • 28
    • 36248954514 scopus 로고    scopus 로고
    • Requirement of left-handed glycine residue for high stability of the Tk-subtilisin propeptide as revealed by mutational and crystallographic analyses
    • Pulido M., Tanaka S., Sringiew C., You D.J., Matsumura H., Koga Y., et al. Requirement of left-handed glycine residue for high stability of the Tk-subtilisin propeptide as revealed by mutational and crystallographic analyses. J. Mol. Biol. 2007, 374:1359-1373.
    • (2007) J. Mol. Biol. , vol.374 , pp. 1359-1373
    • Pulido, M.1    Tanaka, S.2    Sringiew, C.3    You, D.J.4    Matsumura, H.5    Koga, Y.6
  • 29
    • 55749091440 scopus 로고    scopus 로고
    • Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding
    • Tanaka S., Takeuchi Y., Matsumura H., Koga Y., Takano K., Kanaya S. Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding. FEBS Lett. 2008, 582:3875-3878.
    • (2008) FEBS Lett. , vol.582 , pp. 3875-3878
    • Tanaka, S.1    Takeuchi, Y.2    Matsumura, H.3    Koga, Y.4    Takano, K.5    Kanaya, S.6
  • 30
    • 70350536339 scopus 로고    scopus 로고
    • Identification of the interactions critical for propeptide-catalyzed folding of Tk-subtilisin
    • Tanaka S., Matsumura H., Koga Y., Takano K., Kanaya S. Identification of the interactions critical for propeptide-catalyzed folding of Tk-subtilisin. J. Mol. Biol. 2009, 394:306-319.
    • (2009) J. Mol. Biol. , vol.394 , pp. 306-319
    • Tanaka, S.1    Matsumura, H.2    Koga, Y.3    Takano, K.4    Kanaya, S.5
  • 32
    • 77951122723 scopus 로고    scopus 로고
    • Subtilisin-like serine protease from hyperthermophilic archaeon Thermococcus kodakaraensis with N- and C-terminal propeptides
    • Foophow T., Tanaka S., Koga Y., Takano K., Kanaya S. Subtilisin-like serine protease from hyperthermophilic archaeon Thermococcus kodakaraensis with N- and C-terminal propeptides. Protein Eng. Des. Sel. 2010, 23:347-355.
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 347-355
    • Foophow, T.1    Tanaka, S.2    Koga, Y.3    Takano, K.4    Kanaya, S.5
  • 33
    • 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 1995, 3:907-914.
    • (1995) Structure , vol.3 , pp. 907-914
    • Gallagher, T.1    Gilliland, G.2    Wang, L.3    Bryan, P.4
  • 34
    • 0032553556 scopus 로고    scopus 로고
    • The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 Å resolution
    • Jain S.C., Shinde U., Li Y., Inouye M., Berman H.M. The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 Å resolution. J. Mol. Biol. 1998, 284:137-144.
    • (1998) J. Mol. Biol. , vol.284 , pp. 137-144
    • Jain, S.C.1    Shinde, U.2    Li, Y.3    Inouye, M.4    Berman, H.M.5
  • 35
    • 8744220594 scopus 로고    scopus 로고
    • The crystal structure of an oxidatively stable subtilisin-like alkaline serine protease, KP-43, with a C-terminal beta-barrel domain
    • Nonaka T., Fujihashi M., Kita A., Saeki K., Ito S., Horikoshi K., Miki K. The crystal structure of an oxidatively stable subtilisin-like alkaline serine protease, KP-43, with a C-terminal beta-barrel domain. J. Biol. Chem. 2004, 279:47344-47351.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47344-47351
    • Nonaka, T.1    Fujihashi, M.2    Kita, A.3    Saeki, K.4    Ito, S.5    Horikoshi, K.6    Miki, K.7
  • 36
    • 0037647026 scopus 로고    scopus 로고
    • 2.4 Å resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor
    • Holyoak T., Wilson M.A., Fenn T.D., Kettner C.A., Petsko G.A., Fuller R.S., Ringe D. 2.4 Å resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor. Biochemistry 2003, 42:6709-6718.
    • (2003) Biochemistry , vol.42 , pp. 6709-6718
    • Holyoak, T.1    Wilson, M.A.2    Fenn, T.D.3    Kettner, C.A.4    Petsko, G.A.5    Fuller, R.S.6    Ringe, D.7
  • 37
    • 0037743535 scopus 로고    scopus 로고
    • The crystal structure of the proprotein processing proteinase furin explains its stringent specificity
    • Henrich S., Cameron A., Bourenkov G.P., Kiefersauer R., Huber R., Lindberg I., et al. The crystal structure of the proprotein processing proteinase furin explains its stringent specificity. Nat. Struct. Biol. 2003, 10:520-526.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 520-526
    • Henrich, S.1    Cameron, A.2    Bourenkov, G.P.3    Kiefersauer, R.4    Huber, R.5    Lindberg, I.6
  • 38
    • 1542297713 scopus 로고    scopus 로고
    • Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases
    • Holyoak T., Kettner C.A., Petsko G.A., Fuller R.S., Ringe D. Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases. Biochemistry 2004, 43:2412-2421.
    • (2004) Biochemistry , vol.43 , pp. 2412-2421
    • Holyoak, T.1    Kettner, C.A.2    Petsko, G.A.3    Fuller, R.S.4    Ringe, D.5
  • 39
    • 70350444436 scopus 로고    scopus 로고
    • Structural basis for the kexin-like serine protease from Aeromonas sobria as sepsis-causing factor
    • Kobayashi H., Utsunomiya H., Yamanaka H., Sei Y., Katunuma N., Okamoto K., Tsuge H. Structural basis for the kexin-like serine protease from Aeromonas sobria as sepsis-causing factor. J. Biol. Chem. 2009, 284:25655-25663.
    • (2009) J. Biol. Chem. , vol.284 , pp. 25655-25663
    • Kobayashi, H.1    Utsunomiya, H.2    Yamanaka, H.3    Sei, Y.4    Katunuma, N.5    Okamoto, K.6    Tsuge, H.7
  • 40
    • 0028067179 scopus 로고
    • Autoprocessing of prothiolsubtilisin E in which active-site serine 221 is altered to cysteine
    • Li Y., Inouye M. Autoprocessing of prothiolsubtilisin E in which active-site serine 221 is altered to cysteine. J. Biol. Chem. 1994, 269:4169-4174.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4169-4174
    • Li, Y.1    Inouye, M.2
  • 41
    • 0028242912 scopus 로고
    • A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal maturation of pro-Kex2 protease
    • Gluschankof P., Fuller R.S. A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal maturation of pro-Kex2 protease. EMBO J. 1994, 13:2280-2288.
    • (1994) EMBO J. , vol.13 , pp. 2280-2288
    • Gluschankof, P.1    Fuller, R.S.2
  • 42
    • 0032080254 scopus 로고    scopus 로고
    • Regulatory roles of the P domain of the subtilisin-like prohormone convertases
    • Zhou A., Martin S., Lipkind G., LaMendola J., Steiner D.F. Regulatory roles of the P domain of the subtilisin-like prohormone convertases. J. Biol. Chem. 1998, 273:11107-11114.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11107-11114
    • Zhou, A.1    Martin, S.2    Lipkind, G.3    LaMendola, J.4    Steiner, D.F.5
  • 43
    • 0037687421 scopus 로고    scopus 로고
    • Mutational analysis of predicted interactions between the catalytic and P domains of prohormone convertase 3 (PC3/PC1)
    • Ueda K., Lipkind G.M., Zhou A., Zhu X., Kuznetsov A., Philipson L., et al. Mutational analysis of predicted interactions between the catalytic and P domains of prohormone convertase 3 (PC3/PC1). Proc. Natl Acad. Sci. USA 2003, 100:5622-5627.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5622-5627
    • Ueda, K.1    Lipkind, G.M.2    Zhou, A.3    Zhu, X.4    Kuznetsov, A.5    Philipson, L.6
  • 44
    • 0029019483 scopus 로고
    • Pro-sequences assisted protein folding
    • Eder J., Fersht A.R. Pro-sequences assisted protein folding. Mol. Microbiol. 1995, 16:609-614.
    • (1995) Mol. Microbiol. , vol.16 , pp. 609-614
    • Eder, J.1    Fersht, A.R.2
  • 45
    • 0034731382 scopus 로고    scopus 로고
    • Protein engineering of subtilisin
    • Bryan P.N. Protein engineering of subtilisin. Biochim. Biophys. Acta 2000, 1543:203-222.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 203-222
    • Bryan, P.N.1
  • 46
    • 33846411851 scopus 로고    scopus 로고
    • Mechanism of the kinetically-controlled folding reaction of subtilisin
    • Fisher K.E., Ruan B., Alexander P.A., Wang L., Bryan P.N. Mechanism of the kinetically-controlled folding reaction of subtilisin. Biochemistry 2007, 46:640-651.
    • (2007) Biochemistry , vol.46 , pp. 640-651
    • Fisher, K.E.1    Ruan, B.2    Alexander, P.A.3    Wang, L.4    Bryan, P.N.5
  • 47
    • 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 J., Ruvinov S., Strausberg S., Alexander P., et al. Catalysis of a protein folding reaction: mechanistic implications of the 2.0 Å structure of the subtilisin-prodomain complex. Biochemistry 1995, 34:10310-10318.
    • (1995) Biochemistry , vol.34 , pp. 10310-10318
    • Bryan, P.1    Wang, L.2    Hoskins, J.3    Ruvinov, S.4    Strausberg, S.5    Alexander, P.6
  • 48
    • 84871693371 scopus 로고
    • The spectrophotometric determination of tyrosine and tryptophan in proteins
    • Goodwin T.W., Morton R.A. The spectrophotometric determination of tyrosine and tryptophan in proteins. Biochem. J. 1946, 40:628-632.
    • (1946) Biochem. J. , vol.40 , pp. 628-632
    • Goodwin, T.W.1    Morton, R.A.2
  • 49
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 50
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 51
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 1997, 30:1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 52
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 1994, 50:760-763.
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 53
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer G., Cohen S.X., Lamzin V.S., Perrakis A. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 2008, 3:1171-1179.
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 57
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein alignment in three dimensions
    • Krissinel E., Henrick K. Secondary-structure matching (SSM), a new tool for fast protein alignment in three dimensions. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2004, 60:2256-2268.
    • (2004) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.