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Volumn 335, Issue 5, 2004, Pages 1251-1264

Crystal Structure of Fully Ligated Adenylosuccinate Synthetase from Plasmodium falciparum

Author keywords

Adenylosuccinate synthetase; Dimer interface; Hadacidin; Plasmodium falciparum; Purine salvage pathway

Indexed keywords

ADENYLOSUCCINATE SYNTHASE; ASPARTIC ACID; GUANOSINE DIPHOSPHATE; HADACIDIN; INOSINE PHOSPHATE; MAGNESIUM ION; PROTOZOAL PROTEIN;

EID: 0347284265     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.11.036     Document Type: Article
Times cited : (43)

References (41)
  • 2
    • 0030765104 scopus 로고    scopus 로고
    • Metabolic enzymes as potential drug targets in Plasmodium falciparum
    • Subbayya I.N., Ray S.S., Balaram P., Balaram H. Metabolic enzymes as potential drug targets in Plasmodium falciparum. Indian J. Med. Res. 106:1997;79-94.
    • (1997) Indian J. Med. Res. , vol.106 , pp. 79-94
    • Subbayya, I.N.1    Ray, S.S.2    Balaram, P.3    Balaram, H.4
  • 3
    • 0018633747 scopus 로고
    • Biochemistry of Plasmodium (malarial parasites)
    • Sherman I.W. Biochemistry of Plasmodium (malarial parasites). Microbiol. Rev. 43:1979;453-495.
    • (1979) Microbiol. Rev. , vol.43 , pp. 453-495
    • Sherman, I.W.1
  • 4
    • 0037015614 scopus 로고    scopus 로고
    • Genome sequence of the human malaria parasite Plasmodium falciparum
    • Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman H.W., et al. Genome sequence of the human malaria parasite Plasmodium falciparum. Nature. 6906:2002;498-511.
    • (2002) Nature , vol.6906 , pp. 498-511
    • Gardner, M.J.1    Hall, N.2    Fung, E.3    White, O.4    Berriman, M.5    Hyman, H.W.6
  • 5
    • 0034859202 scopus 로고    scopus 로고
    • Development of a bacterial screen for novel hypoxanthine-guanine phosphoribosyltransferase substrates
    • Shivashankar K., Subbayya I.N., Balaram H. Development of a bacterial screen for novel hypoxanthine-guanine phosphoribosyltransferase substrates. J. Mol. Microbiol. Biotechnol. 3:2001;557-562.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 557-562
    • Shivashankar, K.1    Subbayya, I.N.2    Balaram, H.3
  • 6
    • 0033519996 scopus 로고    scopus 로고
    • The 2.0 Å structure of malarial purine phosphoribosyltransferase in complex with a transition-state analog inhibitor
    • Shi W., Li C.M., Tyler P.C., Furneaux R.H., Cahill S.M., Girvin M.E., et al. The 2.0 Å structure of malarial purine phosphoribosyltransferase in complex with a transition-state analog inhibitor. Biochemistry. 38:1999;9872-9880.
    • (1999) Biochemistry , vol.38 , pp. 9872-9880
    • Shi, W.1    Li, C.M.2    Tyler, P.C.3    Furneaux, R.H.4    Cahill, S.M.5    Girvin, M.E.6
  • 7
    • 0033517848 scopus 로고    scopus 로고
    • Crystal structures of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase-GMP and -IMP complexes: Comparison of purine binding interactions with the XMP complex
    • Heroux A., White E.L., Ross L.J., Borhani D.W. Crystal structures of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase-GMP and -IMP complexes: comparison of purine binding interactions with the XMP complex. Biochemistry. 38:1999;14485-14494.
    • (1999) Biochemistry , vol.38 , pp. 14485-14494
    • Heroux, A.1    White, E.L.2    Ross, L.J.3    Borhani, D.W.4
  • 8
    • 0034617303 scopus 로고    scopus 로고
    • Purine phosphoribosyltransferases
    • Craig S.P. 3rd, Eakin A.E. Purine phosphoribosyltransferases. J. Biol. Chem. 275:2000;20231-20234.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20231-20234
    • Craig III, S.P.1    Eakin, A.E.2
  • 9
    • 0036479245 scopus 로고    scopus 로고
    • Purine-less death in Plasmodium falciparum induced by immucillin-H, a transition state analogue of purine nucleoside phosphorylase
    • Kicska G.A., Tyler P.C., Evans G.B., Furneaux R.H., Schramm V.L., Kim K. Purine-less death in Plasmodium falciparum induced by immucillin-H, a transition state analogue of purine nucleoside phosphorylase. J. Biol. Chem. 277:2002;3226-3231.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3226-3231
    • Kicska, G.A.1    Tyler, P.C.2    Evans, G.B.3    Furneaux, R.H.4    Schramm, V.L.5    Kim, K.6
  • 10
    • 0020668139 scopus 로고
    • Regulation, genetics, and properties of adenylosuccinate synthetase: A review
    • Stayton M.M., Rudolph F.B., Fromm H.J. Regulation, genetics, and properties of adenylosuccinate synthetase: a review. Curr. Top. Cell. Regul. 22:1983;103-141.
    • (1983) Curr. Top. Cell. Regul. , vol.22 , pp. 103-141
    • Stayton, M.M.1    Rudolph, F.B.2    Fromm, H.J.3
  • 11
    • 0037470180 scopus 로고    scopus 로고
    • Variations in the response of mouse isozymes of adenylosuccinate synthetase to inhibitors of physiological relevance
    • Borza T., Iancu C.V., Pike E., Honzatko R.B., Fromm H.J. Variations in the response of mouse isozymes of adenylosuccinate synthetase to inhibitors of physiological relevance. J. Biol. Chem. 278:2003;6673-6679.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6673-6679
    • Borza, T.1    Iancu, C.V.2    Pike, E.3    Honzatko, R.B.4    Fromm, H.J.5
  • 12
    • 0023263288 scopus 로고
    • Analysis of sequences from the extremely A+T-rich genome of Plasmodium falciparum
    • Weber J.L. Analysis of sequences from the extremely A+T-rich genome of Plasmodium falciparum. Gene. 52:1987;103-109.
    • (1987) Gene , vol.52 , pp. 103-109
    • Weber, J.L.1
  • 13
    • 0012290107 scopus 로고    scopus 로고
    • Cloning and characterization of the Plasmodium falciparum adenylosuccinate synthetase gene
    • Sumathy K., Jayalakshmi R., Shivayogi M.S., Balaram H. Cloning and characterization of the Plasmodium falciparum adenylosuccinate synthetase gene. Curr. Sci. 78:2000;610-615.
    • (2000) Curr. Sci. , vol.78 , pp. 610-615
    • Sumathy, K.1    Jayalakshmi, R.2    Shivayogi, M.S.3    Balaram, H.4
  • 14
    • 0036930693 scopus 로고    scopus 로고
    • Purification and characterization of recombinant Plasmodium falciparum adenylosuccinate synthetase expressed in Escherichia coli
    • Jayalakshmi R., Sumathy K., Balaram H. Purification and characterization of recombinant Plasmodium falciparum adenylosuccinate synthetase expressed in Escherichia coli. Protein Expr. Purif. 25:2002;65-72.
    • (2002) Protein Expr. Purif. , vol.25 , pp. 65-72
    • Jayalakshmi, R.1    Sumathy, K.2    Balaram, H.3
  • 15
    • 0014690693 scopus 로고
    • Initial rate studies of adenylosuccinate synthetase with product and competitive inhibitors
    • Rudolph F.B., Fromm H.J. Initial rate studies of adenylosuccinate synthetase with product and competitive inhibitors. J. Biol. Chem. 244:1969;3832-3839.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3832-3839
    • Rudolph, F.B.1    Fromm, H.J.2
  • 16
    • 0346705942 scopus 로고    scopus 로고
    • Recombinant mouse muscle adenylosuccinate synthetase: Overexpression, kinetics, and crystal structure
    • Iancu C.V., Borza T., Choe J.Y., Fromm H.J., Honzatko R.B. Recombinant mouse muscle adenylosuccinate synthetase: overexpression, kinetics, and crystal structure. J. Biol. Chem. 276:2001;42146-42152.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42146-42152
    • Iancu, C.V.1    Borza, T.2    Choe, J.Y.3    Fromm, H.J.4    Honzatko, R.B.5
  • 17
    • 19144367977 scopus 로고
    • Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli
    • Silva M.M., Poland B.W., Hoffman C.R., Fromm H.J., Honzatko R.B. Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli. J. Mol. Biol. 254:1995;431-446.
    • (1995) J. Mol. Biol. , vol.254 , pp. 431-446
    • Silva, M.M.1    Poland, B.W.2    Hoffman, C.R.3    Fromm, H.J.4    Honzatko, R.B.5
  • 18
    • 0034681295 scopus 로고    scopus 로고
    • Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana
    • Prade L., Cowan-Jacob S.W., Chemla P., Potter S., Ward E., Fonne-Pfister R. Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana. J. Mol. Biol. 296:2000;569-577.
    • (2000) J. Mol. Biol. , vol.296 , pp. 569-577
    • Prade, L.1    Cowan-Jacob, S.W.2    Chemla, P.3    Potter, S.4    Ward, E.5    Fonne-Pfister, R.6
  • 19
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R.A., Moss D.S., Thornton J.M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231:1993;1049-1067.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 20
    • 0033602925 scopus 로고    scopus 로고
    • Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli
    • Choe J.Y., Poland B.W., Fromm H.J., Honzatko R.B. Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli. Biochemistry. 38:1999;6953-6961.
    • (1999) Biochemistry , vol.38 , pp. 6953-6961
    • Choe, J.Y.1    Poland, B.W.2    Fromm, H.J.3    Honzatko, R.B.4
  • 21
    • 0037178842 scopus 로고    scopus 로고
    • IMP, GTP, and 6-phosphoryl-IMP complexes of recombinant mouse muscle adenylosuccinate synthetase
    • Iancu C.V., Borza T., Fromm H.J., Honzatko R.B. IMP, GTP, and 6-phosphoryl-IMP complexes of recombinant mouse muscle adenylosuccinate synthetase. J. Biol. Chem. 277:2002;26779-26787.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26779-26787
    • Iancu, C.V.1    Borza, T.2    Fromm, H.J.3    Honzatko, R.B.4
  • 22
    • 0030858490 scopus 로고    scopus 로고
    • Relationship of conserved residues in the IMP binding site to substrate recognition and catalysis in Escherichia coli adenylosuccinate synthetase
    • Wang W., Hou Z., Honzatko R.B., Fromm H.J. Relationship of conserved residues in the IMP binding site to substrate recognition and catalysis in Escherichia coli adenylosuccinate synthetase. J. Biol. Chem. 272:1997;16911-16916.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16911-16916
    • Wang, W.1    Hou, Z.2    Honzatko, R.B.3    Fromm, H.J.4
  • 23
    • 0033598677 scopus 로고    scopus 로고
    • Protein-sulphenic acids: Diverse roles of an unlikely player in enzyme catalysis and redox regulation
    • Claiborne A., Yeh J.I., Mallett C., Luba J., Crane E.J., Charrier V., Parsonage D. Protein-sulphenic acids: diverse roles of an unlikely player in enzyme catalysis and redox regulation. Biochemistry. 47:1999;15407-15416.
    • (1999) Biochemistry , vol.47 , pp. 15407-15416
    • Claiborne, A.1    Yeh, J.I.2    Mallett, C.3    Luba, J.4    Crane, E.J.5    Charrier, V.6    Parsonage, D.7
  • 24
    • 0030904928 scopus 로고    scopus 로고
    • A study of Escherichia coli adenylosuccinate synthetase association states and the interface residues of the homodimer
    • Wang W., Gorrell A., Honzatko R.B., Fromm H.J. A study of Escherichia coli adenylosuccinate synthetase association states and the interface residues of the homodimer. J. Biol. Chem. 272:1997;7078-7084.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7078-7084
    • Wang, W.1    Gorrell, A.2    Honzatko, R.B.3    Fromm, H.J.4
  • 25
    • 0037155194 scopus 로고    scopus 로고
    • IMP alone organizes the active site of adenylosuccinate synthetase from Escherichia coli
    • Hou Z., Wang W., Fromm H.J., Honzatko R.B. IMP alone organizes the active site of adenylosuccinate synthetase from Escherichia coli. J. Biol. Chem. 277:2002;5970-5976.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5970-5976
    • Hou, Z.1    Wang, W.2    Fromm, H.J.3    Honzatko, R.B.4
  • 26
    • 0028030684 scopus 로고
    • Low-barrier hydrogen bonds and enzymic catalysis
    • Cleland W.W., Kreevoy M.M. Low-barrier hydrogen bonds and enzymic catalysis. Science. 264:1994;1887-1890.
    • (1994) Science , vol.264 , pp. 1887-1890
    • Cleland, W.W.1    Kreevoy, M.M.2
  • 27
    • 0030009039 scopus 로고    scopus 로고
    • Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli
    • Poland B.W., Hou Z., Bruns C., Fromm H.J., Honzatko R.B. Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli. J. Biol. Chem. 271:1996;15407-15413.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15407-15413
    • Poland, B.W.1    Hou, Z.2    Bruns, C.3    Fromm, H.J.4    Honzatko, R.B.5
  • 28
    • 0021348043 scopus 로고
    • Monophosphates of formycin B and allopurinol riboside. Interactions with leishmanial and mammalian succino-AMP synthetase and GMP reductase
    • Spector T., Jones T.E., LaFon S.W., Nelson D.J., Berens R.L., Marr J.J. Monophosphates of formycin B and allopurinol riboside. Interactions with leishmanial and mammalian succino-AMP synthetase and GMP reductase. Biochem. Pharmacol. 33:1984;1611-1617.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 1611-1617
    • Spector, T.1    Jones, T.E.2    Lafon, S.W.3    Nelson, D.J.4    Berens, R.L.5    Marr, J.J.6
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowsky Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowsky, Z.1    Minor, W.2
  • 30
    • 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
  • 31
    • 0031053055 scopus 로고    scopus 로고
    • AMoRe: An automated molecular replacement program package
    • Navaza J., Saludjian P. AMoRe: an automated molecular replacement program package. Methods Enzymol. 276:1997;581-593.
    • (1997) Methods Enzymol. , vol.276 , pp. 581-593
    • Navaza, J.1    Saludjian, P.2
  • 33
    • 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., Cowan S.W., Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta. Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta. Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 35
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: A program to superimpose protein coordinates accounting for insertions and deletions
    • Cohen G.E. ALIGN: a program to superimpose protein coordinates accounting for insertions and deletions. J. Appl. Crystallog. 30:1997;1160-1161.
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1160-1161
    • Cohen, G.E.1
  • 36
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 37
    • 0003742069 scopus 로고
    • London: Department of Biochemistry and Molecular Biology, University College
    • Hubbard S.J., Thornton J.M. NACCESS, Computer Program. 1993;Department of Biochemistry and Molecular Biology, University College, London.
    • (1993) NACCESS, Computer Program
    • Hubbard, S.J.1    Thornton, J.M.2
  • 38
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. 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.J.1
  • 39
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 40
    • 0034791613 scopus 로고    scopus 로고
    • CHROMA: Consensus-based colouring of multiple alignments for publication
    • Goodstadt L., Ponting C.P. CHROMA: consensus-based colouring of multiple alignments for publication. Bioinformatics. 17:2001;845-846.
    • (2001) Bioinformatics , vol.17 , pp. 845-846
    • Goodstadt, L.1    Ponting, C.P.2


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