메뉴 건너뛰기




Volumn 6, Issue 2, 1997, Pages 444-449

Expression, purification from inclusion bodies, and crystal characterization of a transition state analog complex of arginine kinase: A model for studying phosphagen kinases

Author keywords

arginine kinase; crystals; expression; guanidino kinase; high resolution; phosphagen kinase; transition state complex

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ARGININE KINASE; CREATINE KINASE; GUANIDINE DERIVATIVE; RECOMBINANT PROTEIN;

EID: 0031048875     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060222     Document Type: Article
Times cited : (20)

References (52)
  • 5
    • 0018276787 scopus 로고
    • Creatine kinase. A new crystal form providing evidence of subunit structural homogeneity
    • Burgess AN, Liddell JM, Cook W, Tweedle RM, Swan IDA. 1978. Creatine kinase. A new crystal form providing evidence of subunit structural homogeneity. J Mol Biol 123:691-695.
    • (1978) J Mol Biol , vol.123 , pp. 691-695
    • Burgess, A.N.1    Liddell, J.M.2    Cook, W.3    Tweedle, R.M.4    Swan, I.D.A.5
  • 6
    • 0002944634 scopus 로고
    • Design of crystallization experiments and protocols
    • Ducruix A, Giegé R, eds. Oxford: IRL Press
    • Carter CW. 1992. Design of crystallization experiments and protocols. In: Ducruix A, Giegé R, eds. Crystallization of nucleic acids and proteins. Oxford: IRL Press.
    • (1992) Crystallization of Nucleic Acids and Proteins
    • Carter, C.W.1
  • 7
    • 0027109260 scopus 로고
    • Microbatch crystallization under oil - A new technique allowing many small-volume crystallization trials
    • Chayen NE, Stewart PDS, Blow DM. 1992. Microbatch crystallization under oil - A new technique allowing many small-volume crystallization trials. J Crystal Growth 122:176-180.
    • (1992) J Crystal Growth , vol.122 , pp. 176-180
    • Chayen, N.E.1    Stewart, P.D.S.2    Blow, D.M.3
  • 10
    • 0027486802 scopus 로고
    • Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle
    • Dumas C, Camonis J. 1993. Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle. J Biol Chem 265:21599-21606.
    • (1993) J Biol Chem , vol.265 , pp. 21599-21606
    • Dumas, C.1    Camonis, J.2
  • 11
    • 0016802401 scopus 로고
    • A quenched-flow study of the reaction catalysed by creatine kinase
    • Engelborghs Y, Marsh A, Gutfreund H. 1975. A quenched-flow study of the reaction catalysed by creatine kinase. Biochem J 151:47-50.
    • (1975) Biochem J , vol.151 , pp. 47-50
    • Engelborghs, Y.1    Marsh, A.2    Gutfreund, H.3
  • 12
    • 0030606976 scopus 로고    scopus 로고
    • Changes of creatine kinase structure upon ligand binding as seen by small-angle scattering
    • Forstner M, Kriechbaum M, Laggner MP, Wallimann T. 1996. Changes of creatine kinase structure upon ligand binding as seen by small-angle scattering. J Mol Struct 383:217.
    • (1996) J Mol Struct , vol.383 , pp. 217
    • Forstner, M.1    Kriechbaum, M.2    Laggner, M.P.3    Wallimann, T.4
  • 13
    • 0030063376 scopus 로고    scopus 로고
    • Denaturation and urea gradient gel electrophoresis of arginine kinase: Evidence for a collapsed-state conformation
    • France RM, Grossman SH. 1996. Denaturation and urea gradient gel electrophoresis of arginine kinase: Evidence for a collapsed-state conformation. Arch Biochem Biophys 326:93-99.
    • (1996) Arch Biochem Biophys , vol.326 , pp. 93-99
    • France, R.M.1    Grossman, S.H.2
  • 15
    • 0021095858 scopus 로고
    • Crystallization and preliminary X-ray diffraction data of two crystal forms of bovine heart creatine kinase
    • Gilliland GL, Sjölin L, Olsson G. 1983. Crystallization and preliminary X-ray diffraction data of two crystal forms of bovine heart creatine kinase. J Mol Biol 170:791-793.
    • (1983) J Mol Biol , vol.170 , pp. 791-793
    • Gilliland, G.L.1    Sjölin, L.2    Olsson, G.3
  • 16
    • 0028246759 scopus 로고
    • The Tryptophan residues of mitochondrial creatine kinase: Roles of Trp-233, Trp-206, and Trp-264 in active-site and quaternary structure formation
    • Gross M, Furter-Graves EM, Wallimann T, Eppenberger HM, Furter R. 1994. The Tryptophan residues of mitochondrial creatine kinase: Roles of Trp-233, Trp-206, and Trp-264 in active-site and quaternary structure formation. Protein Sci 3:1058-1068.
    • (1994) Protein Sci , vol.3 , pp. 1058-1068
    • Gross, M.1    Furter-Graves, E.M.2    Wallimann, T.3    Eppenberger, H.M.4    Furter, R.5
  • 17
    • 0019888151 scopus 로고
    • The stereochemical course of the reaction catalyzed by creatine kinase
    • Hansen DE, Knowles JR. 1981. The stereochemical course of the reaction catalyzed by creatine kinase. J Biol Chem 256:5967-5969.
    • (1981) J Biol Chem , vol.256 , pp. 5967-5969
    • Hansen, D.E.1    Knowles, J.R.2
  • 18
    • 0022974985 scopus 로고
    • Purification and crystallization of creatine kinase from rabbit skeletal muscle
    • Hershenson S, Helmers N, Desmueles P, Stroud R. 1986. Purification and crystallization of creatine kinase from rabbit skeletal muscle. J Biol Chem 261:3732-3736.
    • (1986) J Biol Chem , vol.261 , pp. 3732-3736
    • Hershenson, S.1    Helmers, N.2    Desmueles, P.3    Stroud, R.4
  • 19
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik J, Kim S-H. 1991. Sparse matrix sampling: A screening method for crystallization of proteins. J Appl Crystallogr 24:409-11.
    • (1991) J Appl Crystallogr , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.-H.2
  • 20
    • 0001662165 scopus 로고
    • Effect of chemical impurities in polyethylene glycol on macromolecular crystallization
    • Jurnak F. 1986. Effect of chemical impurities in polyethylene glycol on macromolecular crystallization. J Crystal Growth 76:577-582.
    • (1986) J Crystal Growth , vol.76 , pp. 577-582
    • Jurnak, F.1
  • 21
    • 0020654939 scopus 로고
    • Creatine kinase: Structure-activity relationships
    • Kenyon GL, Reed GH. 1983. Creatine kinase: Structure-activity relationships. Adv Enzymol 54:367-426.
    • (1983) Adv Enzymol , vol.54 , pp. 367-426
    • Kenyon, G.L.1    Reed, G.H.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during assembly of the head bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0025068606 scopus 로고
    • Transition-state analogues in protein crystallography: Probes of the structural source of enzyme catalysis
    • Lolis E, Petsko G. 1990. Transition-state analogues in protein crystallography: Probes of the structural source of enzyme catalysis. Annu Rev Biochem 59:597-630.
    • (1990) Annu Rev Biochem , vol.59 , pp. 597-630
    • Lolis, E.1    Petsko, G.2
  • 24
    • 0013866009 scopus 로고
    • Cooperative effects of substrates and substrate analogs on the conformation of creatine phosphokinase
    • Lui NST, Cunningham L. 1966. Cooperative effects of substrates and substrate analogs on the conformation of creatine phosphokinase. Biochemistry 5:144-149.
    • (1966) Biochemistry , vol.5 , pp. 144-149
    • Lui, N.S.T.1    Cunningham, L.2
  • 25
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. 1968. Solvent content of protein crystals. J Mol Biol 33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 28
    • 0015805738 scopus 로고
    • A preliminary crystallographic investigation of rabbit muscle creatine kinase
    • McPherson A Jr. 1973. A preliminary crystallographic investigation of rabbit muscle creatine kinase. J Mol Biol 82:83-86.
    • (1973) J Mol Biol , vol.82 , pp. 83-86
    • McPherson Jr., A.1
  • 29
    • 0015052797 scopus 로고
    • Inhibition of adenosine 5′-triphosphatecreatine phosphotransferase by substrate-anion complexes - Evidence for the transition-state organization of the catalytic site
    • Milner-White EJ, Watts DC. 1971. Inhibition of adenosine 5′-triphosphatecreatine phosphotransferase by substrate-anion complexes - Evidence for the transition-state organization of the catalytic site. Biochem J 122:727-740.
    • (1971) Biochem J , vol.122 , pp. 727-740
    • Milner-White, E.J.1    Watts, D.C.2
  • 30
    • 0004202165 scopus 로고
    • West Lafayette: Purdue University
    • Minor W. 1993. XDisplayF Program. West Lafayette: Purdue University.
    • (1993) XDisplayF Program
    • Minor, W.1
  • 31
    • 77956932220 scopus 로고
    • Arginine kinase and other invertebrate guanidino kinases
    • Boyer PD, ed. New York: Academic Press
    • Morrison JF. 1973. Arginine kinase and other invertebrate guanidino kinases. In: Boyer PD, ed. The enzymes. Vol. 8. New York: Academic Press, pp 457-486.
    • (1973) The Enzymes , vol.8 , pp. 457-486
    • Morrison, J.F.1
  • 33
    • 0342932475 scopus 로고
    • Data collection and processing
    • Henrick K, Moss DS, Tickle IJ, eds. Daresbury, England: Daresbury Laboratory
    • Otwinowski Z. 1990. Data collection and processing. In: Henrick K, Moss DS, Tickle IJ, eds. Proceedings of the CCP4 study weekend. Daresbury, England: Daresbury Laboratory, pp 73-82.
    • (1990) Proceedings of the CCP4 Study Weekend , pp. 73-82
    • Otwinowski, Z.1
  • 34
    • 0028809374 scopus 로고
    • Polymeric precipitants for the crystallization of macromolecules
    • Patel S, Cudney B, McPherson A. 1995. Polymeric precipitants for the crystallization of macromolecules. Biochem Biophys Res Commun 207:819-829.
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 819-829
    • Patel, S.1    Cudney, B.2    McPherson, A.3
  • 36
    • 0021863643 scopus 로고
    • A simple procedure for removing contaminating aldehydes and peroxides from aqueous solutions of polyethylene glycols and of nonionic detergents that are based on the polyoxyethylene linkage
    • Ray WJ, Puvathingal J. 1985. A simple procedure for removing contaminating aldehydes and peroxides from aqueous solutions of polyethylene glycols and of nonionic detergents that are based on the polyoxyethylene linkage. Ann Biochem 146:307.
    • (1985) Ann Biochem , vol.146 , pp. 307
    • Ray, W.J.1    Puvathingal, J.2
  • 37
    • 0015523053 scopus 로고
    • Structural changes induced by substrates and anions at the active site of creatine kinase
    • Reed GH, Cohn M. 1972. Structural changes induced by substrates and anions at the active site of creatine kinase. J Biol Chem 247:3073-3081.
    • (1972) J Biol Chem , vol.247 , pp. 3073-3081
    • Reed, G.H.1    Cohn, M.2
  • 38
    • 0028774714 scopus 로고
    • Cryocrystallography
    • Rodgers DW. 1994. Cryocrystallography. Structure 2:1135-1140.
    • (1994) Structure , vol.2 , pp. 1135-1140
    • Rodgers, D.W.1
  • 40
    • 0025687007 scopus 로고
    • Crystallization and preliminary X-ray analysis of two different forms of mitochondrial creatine kinase from chicken cardiac muscle
    • Schnyder T, Sargent DF, Richmond TJ, Eppenberger HM, Wallimann T. 1990. Crystallization and preliminary X-ray analysis of two different forms of mitochondrial creatine kinase from chicken cardiac muscle. J Mol Biol 216:809-812.
    • (1990) J Mol Biol , vol.216 , pp. 809-812
    • Schnyder, T.1    Sargent, D.F.2    Richmond, T.J.3    Eppenberger, H.M.4    Wallimann, T.5
  • 41
    • 0025754308 scopus 로고
    • Crystallization of mitochondrial creatine kinase: Growing of large protein crystals and electron microscopic investigation of microcrystals consisting of octamers
    • Schnyder T, Winkler H, Gross H, Eppenberger HM, Wallimann, T. 1991. Crystallization of mitochondrial creatine kinase: Growing of large protein crystals and electron microscopic investigation of microcrystals consisting of octamers. J Biol Chem 266:5318-5322.
    • (1991) J Biol Chem , vol.266 , pp. 5318-5322
    • Schnyder, T.1    Winkler, H.2    Gross, H.3    Eppenberger, H.M.4    Wallimann, T.5
  • 42
    • 0342932465 scopus 로고
    • Predispensed gradient matrices - A new rapid method of finding crystallization conditions
    • Stewart PDS, Khimasia M. 1994. Predispensed gradient matrices - A new rapid method of finding crystallization conditions. Acta Crystallogr D50:441-442.
    • (1994) Acta Crystallogr , vol.D50 , pp. 441-442
    • Stewart, P.D.S.1    Khimasia, M.2
  • 44
    • 0027133018 scopus 로고
    • Horseshoe crab sperm contain a unique isoform of arginine kinase that is present in midpiece and flagellum
    • Strong SJ, Ellington WR. 1993. Horseshoe crab sperm contain a unique isoform of arginine kinase that is present in midpiece and flagellum. J Exp Zool 267:563-571.
    • (1993) J Exp Zool , vol.267 , pp. 563-571
    • Strong, S.J.1    Ellington, W.R.2
  • 45
    • 0028858939 scopus 로고
    • Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: Insights into catalytically important residues
    • Strong SJ, Ellington WR. 1995. Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: Insights into catalytically important residues. BiochimBiophys Acta 1246:197-200.
    • (1995) BiochimBiophys Acta , vol.1246 , pp. 197-200
    • Strong, S.J.1    Ellington, W.R.2
  • 46
    • 0029888809 scopus 로고    scopus 로고
    • Expression of horseshoe crab arginine kinase in Escherichia coli and site directed mutations of the reactive cysteine peptide
    • Strong SJ, Ellington WR. 1996. Expression of horseshoe crab arginine kinase in Escherichia coli and site directed mutations of the reactive cysteine peptide. Comp Biochem Physiol 113B:809-816.
    • (1996) Comp Biochem Physiol , vol.113 B , pp. 809-816
    • Strong, S.J.1    Ellington, W.R.2
  • 47
    • 0028212764 scopus 로고
    • Evolution of phosphagen kinase: Primary structure of glycocyamine kinase and arginine kinase from invertebrates
    • Suzuki T, Furukohri T. 1994. Evolution of phosphagen kinase: Primary structure of glycocyamine kinase and arginine kinase from invertebrates. J Mol Biol 257:353-357.
    • (1994) J Mol Biol , vol.257 , pp. 353-357
    • Suzuki, T.1    Furukohri, T.2
  • 48
    • 0021843865 scopus 로고
    • Metabolite channeling: A phosphorylcreatine shuttle to mediate high energy phosphate transport between sperm mitochondrion and tail
    • Tombes RM, Shapiro BM. 1985. Metabolite channeling: A phosphorylcreatine shuttle to mediate high energy phosphate transport between sperm mitochondrion and tail. Cell 47:325-344.
    • (1985) Cell , vol.47 , pp. 325-344
    • Tombes, R.M.1    Shapiro, B.M.2
  • 49
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes: The "phospho-creatine circuit" for cellular energy homeostasis
    • Wallimann T, Wyss M, Brdiczka D, Nicolay K, Eppenberger HM. 1992. Intracellular compartmentation, structure and function of creatine kinase isoenzymes: The "phospho-creatine circuit" for cellular energy homeostasis. Biochem J 281:21-40.
    • (1992) Biochem J , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 50
    • 77956904558 scopus 로고
    • Creatine kinase (adenosine 5′-triphosphate-creatine phosphotransferase)
    • Boyer PD, ed. New York: Academic Press
    • Watts DC. 1973. Creatine kinase (adenosine 5′-triphosphate-creatine phosphotransferase). In: Boyer PD, ed. The enzymes. Vol. 8. New York: Academic Press. pp 383-455.
    • (1973) The Enzymes , vol.8 , pp. 383-455
    • Watts, D.C.1
  • 51
    • 0029610598 scopus 로고
    • Direct sequence data from heterogeneous creatine kinase (43 kDa) by high-resolution tandem mass spectrometry
    • Wood TW, Chen LH, Kelleher NL, Little DP, Kenyon GL, McLafferty FW. 1995. Direct sequence data from heterogeneous creatine kinase (43 kDa) by high-resolution tandem mass spectrometry. Biochemistry 34:16251-16254.
    • (1995) Biochemistry , vol.34 , pp. 16251-16254
    • Wood, T.W.1    Chen, L.H.2    Kelleher, N.L.3    Little, D.P.4    Kenyon, G.L.5    McLafferty, F.W.6
  • 52
    • 0029916225 scopus 로고    scopus 로고
    • Control of aggregation in protein refolding: The temperature-leap tactic
    • Xie Y, Wetlaufer DB. 1996. Control of aggregation in protein refolding: The temperature-leap tactic. Protein Sci 5:517-523.
    • (1996) Protein Sci , vol.5 , pp. 517-523
    • Xie, Y.1    Wetlaufer, D.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.