메뉴 건너뛰기




Volumn 282, Issue 4, 1998, Pages 875-889

Structures of free and complexed forms of Escherichia coli xanthine-guanine phosphoribosyltransferase

Author keywords

Enzyme ligand complexes; Phosphoribosyltransferases; Protein structure; Purine salvage; X ray crystallography

Indexed keywords

GUANINE; MAGNESIUM; PHOSPHORIBOSYLTRANSFERASE; PROTON; SULFATE; XANTHINE;

EID: 0032475913     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2051     Document Type: Article
Times cited : (57)

References (50)
  • 1
    • 0022994953 scopus 로고
    • Purification and characterisation of guanine phosphoribosyltransferase from Giardia lamblia
    • Aldritt S.M., Wang C.C. Purification and characterisation of guanine phosphoribosyltransferase from Giardia lamblia. J. Biol. Chem. 261:1986;8528-8533
    • (1986) J. Biol. Chem. , vol.261 , pp. 8528-8533
    • Aldritt, S.M.1    Wang, C.C.2
  • 2
    • 0027438369 scopus 로고
    • Cloning and expression of the hypoxanthine-guanine phosphoribosyltransferase gene from Trypanosoma brucei
    • Allen T.E., Ullman B. Cloning and expression of the hypoxanthine-guanine phosphoribosyltransferase gene from Trypanosoma brucei. Nucl. Acids Res. 21:1993;5431-5438
    • (1993) Nucl. Acids Res. , vol.21 , pp. 5431-5438
    • Allen, T.E.1    Ullman, B.2
  • 3
    • 0028206197 scopus 로고
    • Molecular characterisation and overexpression of the hypoxanthine-guanine phosphoribosyltransferase gene from Trypanosoma cruzi
    • Allen T.E., Ullman B. Molecular characterisation and overexpression of the hypoxanthine-guanine phosphoribosyltransferase gene from Trypanosoma cruzi. Mol. Biochem. Parasitol. 65:1994;233-245
    • (1994) Mol. Biochem. Parasitol. , vol.65 , pp. 233-245
    • Allen, T.E.1    Ullman, B.2
  • 4
    • 0024592784 scopus 로고
    • Purification and characterisation of the adenine phosphoribosyltransferase and hypoxanthine-guanine phosphoribosyltransferase activities from Leishmania donovani
    • Allen T., Henschel E.V., Coons T., Cross L., Conley J., Ullman B. Purification and characterisation of the adenine phosphoribosyltransferase and hypoxanthine-guanine phosphoribosyltransferase activities from Leishmania donovani. Mol. Biochem. Parasitol. 33:1989;273-282
    • (1989) Mol. Biochem. Parasitol. , vol.33 , pp. 273-282
    • Allen, T.1    Henschel, E.V.2    Coons, T.3    Cross, L.4    Conley, J.5    Ullman, B.6
  • 5
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space filling molecular pictures
    • Bacon D.J., Anderson W.F. A fast algorithm for rendering space filling molecular pictures. J. Mol. Graph. 6:1988;219-222
    • (1988) J. Mol. Graph. , vol.6 , pp. 219-222
    • Bacon, D.J.1    Anderson, W.F.2
  • 6
    • 0027216310 scopus 로고
    • The hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus has unique properties
    • Beck J.T., Wang C.C. The hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus has unique properties. Mol. Biochem. Parasitol. 60:1993;187-194
    • (1993) Mol. Biochem. Parasitol. , vol.60 , pp. 187-194
    • Beck, J.T.1    Wang, C.C.2
  • 7
    • 0021470578 scopus 로고
    • OMITMAP: An electron density map suitable for the examination of errors in a macromolecular model
    • Bhat T.N., Cohen G.H. OMITMAP an electron density map suitable for the examination of errors in a macromolecular model. J. Appl. Crystallog. 17:1984;244-248
    • (1984) J. Appl. Crystallog. , vol.17 , pp. 244-248
    • Bhat, T.N.1    Cohen, G.H.2
  • 9
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A.T. The free R value a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 10
    • 0030772416 scopus 로고    scopus 로고
    • Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides
    • Chen S., Tomchick D.R., Wolle D., Hu P., Smith J.L., Switzer R.L., Zalkin H. Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides. Biochemistry. 36:1997;10718-10726
    • (1997) Biochemistry , vol.36 , pp. 10718-10726
    • Chen, S.1    Tomchick, D.R.2    Wolle, D.3    Hu, P.4    Smith, J.L.5    Switzer, R.L.6    Zalkin, H.7
  • 12
    • 0021848247 scopus 로고
    • Purification and characterisation of Escherichia coli xanthine-guanine phosphoribosyltransferase produced by plasmid pSV2gpt
    • Deo S.S., Tseng W.C., Saini R., Coles R.S., Athwal R.S. Purification and characterisation of Escherichia coli xanthine-guanine phosphoribosyltransferase produced by plasmid pSV2gpt. Biochim. Biophys. Acta. 839:1985;233-239
    • (1985) Biochim. Biophys. Acta , vol.839 , pp. 233-239
    • Deo, S.S.1    Tseng, W.C.2    Saini, R.3    Coles, R.S.4    Athwal, R.S.5
  • 13
    • 0028083309 scopus 로고
    • The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP
    • Eads J.C., Scapin G., Xu Y., Grubmeyer C., Sacchettini J.C. The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell. 78:1994;325-334
    • (1994) Cell , vol.78 , pp. 325-334
    • Eads, J.C.1    Scapin, G.2    Xu, Y.3    Grubmeyer, C.4    Sacchettini, J.C.5
  • 14
    • 0031568330 scopus 로고    scopus 로고
    • A new function for a common fold: The crystal structure of quinolinic acid phosphoribosyltransferase
    • Eads J.C., Ozturk D., Wexler T.B., Grubmeyer C., Sacchettini J.C. A new function for a common fold the crystal structure of quinolinic acid phosphoribosyltransferase. Structure. 5:1997;47-58
    • (1997) Structure , vol.5 , pp. 47-58
    • Eads, J.C.1    Ozturk, D.2    Wexler, T.B.3    Grubmeyer, C.4    Sacchettini, J.C.5
  • 15
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans S.V. SETOR hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11:1993;134-138
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 16
    • 0018177022 scopus 로고
    • Human hypoxanthine-guanine phosphoribosyltransferase. Steady state kinetics of the forward and reverse reactions
    • Giacomello A., Salerno C. Human hypoxanthine-guanine phosphoribosyltransferase. Steady state kinetics of the forward and reverse reactions. J. Biol. Chem. 253:1978;6038-6044
    • (1978) J. Biol. Chem. , vol.253 , pp. 6038-6044
    • Giacomello, A.1    Salerno, C.2
  • 17
    • 0017904809 scopus 로고
    • 3H substrate kinetic isotope effects for some phosphoribosyltransferases
    • 3H substrate kinetic isotope effects for some phosphoribosyltransferases. J. Biol. Chem. 253:1978;2963-2971
    • (1978) J. Biol. Chem. , vol.253 , pp. 2963-2971
    • Goitein, R.K.1    Chelsky, D.2    Parsons, S.M.3
  • 18
    • 0029990345 scopus 로고    scopus 로고
    • A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase
    • Henriksen A., Aghajari N., Jensen K.F., Gajhede M. A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase. Biochemistry. 35:1996;3803-3809
    • (1996) Biochemistry , vol.35 , pp. 3803-3809
    • Henriksen, A.1    Aghajari, N.2    Jensen, K.F.3    Gajhede, M.4
  • 19
    • 0022456388 scopus 로고
    • Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyltransferase and comparison with other analogous enzymes
    • Hershey H.V., Taylor M.W. Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyltransferase and comparison with other analogous enzymes. Gene. 43:1986;287-293
    • (1986) Gene , vol.43 , pp. 287-293
    • Hershey, H.V.1    Taylor, M.W.2
  • 21
    • 0022837418 scopus 로고
    • Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of the purified enzyme and primary structure of the prs gene
    • Hove-Jensen B., Harlow K.W., King C.J., Switzer R.L. Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of the purified enzyme and primary structure of the prs gene. J. Biol. Chem. 261:1986;6765-6771
    • (1986) J. Biol. Chem. , vol.261 , pp. 6765-6771
    • Hove-Jensen, B.1    Harlow, K.W.2    King, C.J.3    Switzer, R.L.4
  • 22
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF- a program to identify and analyse structural motifs in proteins
    • Hutchinson E.G., Thornton J.M. PROMOTIF- a program to identify and analyse structural motifs in proteins. Protein Sci. 5:1996;212-220
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 23
    • 0030909604 scopus 로고    scopus 로고
    • The conserved serine-tyrosine dipeptide in Leishmania donovani hypoxanthine-guanine phosphoribosyltransferase is essential for catalytic activity
    • Jardim A., Ullman B. The conserved serine-tyrosine dipeptide in Leishmania donovani hypoxanthine-guanine phosphoribosyltransferase is essential for catalytic activity. J. Biol. Chem. 272:1997;8967-8973
    • (1997) J. Biol. Chem. , vol.272 , pp. 8967-8973
    • Jardim, A.1    Ullman, B.2
  • 24
    • 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 M. 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    Kjeldgaard, M.4
  • 25
    • 0029920154 scopus 로고    scopus 로고
    • Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site
    • Kim J.H., Krahn J.M., Tomchick D.R., Smith J.L., Zalkin H. Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site. J. Biol. Chem. 271:1996;15549-15557
    • (1996) J. Biol. Chem. , vol.271 , pp. 15549-15557
    • Kim, J.H.1    Krahn, J.M.2    Tomchick, D.R.3    Smith, J.L.4    Zalkin, H.5
  • 26
    • 0342894815 scopus 로고    scopus 로고
    • Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site
    • Krahn J.M., Kim J.H., Burns M.R., Parry R.J., Zalkin H., Smith J.L. Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site. Biochemistry. 36:1997;11061-11068
    • (1997) Biochemistry , vol.36 , pp. 11061-11068
    • Krahn, J.M.1    Kim, J.H.2    Burns, M.R.3    Parry, R.J.4    Zalkin, H.5    Smith, J.L.6
  • 27
    • 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
  • 29
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati V. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5:1952;802-810
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 30
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 31
    • 0028057108 scopus 로고
    • Raster3D version 2.0. a program for photorealistic molecular graphics
    • Merritt E.A., Murphy M.E.P. Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-873
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 32
    • 0019748203 scopus 로고
    • Structural features of the phosphoribosyltransferases and their relationship to the human deficiency disorders of purine and pyrimidine metabolism
    • Musick W.D.L. Structural features of the phosphoribosyltransferases and their relationship to the human deficiency disorders of purine and pyrimidine metabolism. CRC Crit. Rev. Biochem. 11:1981;1-34
    • (1981) CRC Crit. Rev. Biochem. , vol.11 , pp. 1-34
    • Musick, W.D.L.1
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Jr. Carter, Sweet R.M. New York: Academic Press
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Carter C.W. Jr, Sweet R.M. Methods in Enzymology. vol. 276:1997;307-326 Academic Press, New York
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 0029150167 scopus 로고
    • Locations and functional roles of conserved lysine residues in Salmonella typhimurium orotate phosphoribosyltransferase
    • Ozturk D.H., Dorfman R.H., Scapin G., Sacchettini J.C., Grubmeyer C. Locations and functional roles of conserved lysine residues in Salmonella typhimurium orotate phosphoribosyltransferase. Biochemistry. 34:1995;10755-10763
    • (1995) Biochemistry , vol.34 , pp. 10755-10763
    • Ozturk, D.H.1    Dorfman, R.H.2    Scapin, G.3    Sacchettini, J.C.4    Grubmeyer, C.5
  • 36
    • 0029132683 scopus 로고
    • Structure and function of Salmonella typhimurium orotate phosphoribosyltransferase: Protein complementation reveals shared active sites
    • Ozturk D.H., Dorfman R.H., Scapin G., Sacchettini J.C., Grubmeyer C. Structure and function of Salmonella typhimurium orotate phosphoribosyltransferase protein complementation reveals shared active sites. Biochemistry. 34:1995;10764-10770
    • (1995) Biochemistry , vol.34 , pp. 10764-10770
    • Ozturk, D.H.1    Dorfman, R.H.2    Scapin, G.3    Sacchettini, J.C.4    Grubmeyer, C.5
  • 37
    • 0030905197 scopus 로고    scopus 로고
    • Synthesis of (+)-(1S)-1-pyrophosphoryl-(2R,3R)-2,3-dihydroxy-(4S)-4-(phosphoryloxymethyl) cyclopentane, a stable, optically-active carbocyclic analog of 5-phosphoribosyl-1-pyro phosphate (PRPP)
    • Parry R.J., Burns M.R., Jiralerspong S., Alemany L. Synthesis of (+)-(1S)-1-pyrophosphoryl-(2R,3R)-2,3-dihydroxy-(4S)-4-(phosphoryloxymethyl) cyclopentane, a stable, optically-active carbocyclic analog of 5-phosphoribosyl-1-pyro phosphate (PRPP). Tetrahedron. 53:1997;7077-7088
    • (1997) Tetrahedron , vol.53 , pp. 7077-7088
    • Parry, R.J.1    Burns, M.R.2    Jiralerspong, S.3    Alemany, L.4
  • 38
    • 0023740507 scopus 로고
    • Properties and substrate specificity of a purine phosphoribosyltransferase from the human malaria parasite, Plasmodium falciparum
    • Queen S.A., van der Jagt D., Reyes P. Properties and substrate specificity of a purine phosphoribosyltransferase from the human malaria parasite, Plasmodium falciparum. Mol. Biochem. Parasitol. 30:1988;123-134
    • (1988) Mol. Biochem. Parasitol. , vol.30 , pp. 123-134
    • Queen, S.A.1    Van Der Jagt, D.2    Reyes, P.3
  • 40
    • 0028281205 scopus 로고
    • Crystal structure of orotate phosphoribosyltransferase
    • Scapin G., Grubmeyer C., Sacchettini J.C. Crystal structure of orotate phosphoribosyltransferase. Biochemistry. 33:1994;1287-1294
    • (1994) Biochemistry , vol.33 , pp. 1287-1294
    • Scapin, G.1    Grubmeyer, C.2    Sacchettini, J.C.3
  • 41
    • 0029143903 scopus 로고
    • The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and α-D-5-phosphoribosyl-1-pyrophosphate
    • Scapin G., Ozturk D.H., Grubmeyer C., Sacchettini J.C. The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and α-D-5-phosphoribosyl-1-pyrophosphate. Biochemistry. 34:1995;10744-10754
    • (1995) Biochemistry , vol.34 , pp. 10744-10754
    • Scapin, G.1    Ozturk, D.H.2    Grubmeyer, C.3    Sacchettini, J.C.4
  • 42
    • 0029742013 scopus 로고    scopus 로고
    • Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop
    • Schumacher M.A., Carter D., Roos D.S., Ullman B., Brennan R.G. Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop. Nat. Struct. Biol. 3:1996;881-887
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 881-887
    • Schumacher, M.A.1    Carter, D.2    Roos, D.S.3    Ullman, B.4    Brennan, R.G.5
  • 44
    • 0029898439 scopus 로고    scopus 로고
    • Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus
    • Somoza J.R., Chin M.S., Focia P.J., Wang C.C., Fletterick R.J. Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus. Biochemistry. 35:1996;7032-7040
    • (1996) Biochemistry , vol.35 , pp. 7032-7040
    • Somoza, J.R.1    Chin, M.S.2    Focia, P.J.3    Wang, C.C.4    Fletterick, R.J.5
  • 45
    • 0030070827 scopus 로고    scopus 로고
    • Transition state structure of Salmonella typhimurium orotate phosphoribosyltransferase
    • Tao W., Grubmeyer C., Blanchard J.S. Transition state structure of Salmonella typhimurium orotate phosphoribosyltransferase. Biochemistry. 35:1996;14-21
    • (1996) Biochemistry , vol.35 , pp. 14-21
    • Tao, W.1    Grubmeyer, C.2    Blanchard, J.S.3
  • 46
    • 0029931489 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies of Escherichia coli xanthine phosphoribosyltransferase
    • Vos S., de Jersey J., Martin J.L. Crystallization and preliminary X-ray crystallographic studies of Escherichia coli xanthine phosphoribosyltransferase. J. Struct. Biol. 116:1996;330-334
    • (1996) J. Struct. Biol. , vol.116 , pp. 330-334
    • Vos, S.1    De Jersey, J.2    Martin, J.L.3
  • 47
    • 0030950226 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli xanthine phosphoribosyltransferase
    • Vos S., de Jersey J., Martin J.L. Crystal structure of Escherichia coli xanthine phosphoribosyltransferase. Biochemistry. 36:1997;4125-4134
    • (1997) Biochemistry , vol.36 , pp. 4125-4134
    • Vos, S.1    De Jersey, J.2    Martin, J.L.3
  • 48
    • 0342343943 scopus 로고
    • Purine metabolism in the protozoan parasite Eimeria tenella
    • Wang C.C., Simashkevich P.M. Purine metabolism in the protozoan parasite Eimeria tenella. Proc. Natl Acad. Sci. USA. 78:1981;6618-6622
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 6618-6622
    • Wang, C.C.1    Simashkevich, P.M.2
  • 49
    • 0030883755 scopus 로고    scopus 로고
    • Protein domain movements: Detection of rigid domains and visualization of hinges in comparisons of atomic coordinates
    • Wriggers W., Schulten K. Protein domain movements detection of rigid domains and visualization of hinges in comparisons of atomic coordinates. Proteins: Struct. Funct. Genet. 29:1997;1-14
    • (1997) Proteins: Struct. Funct. Genet. , vol.29 , pp. 1-14
    • Wriggers, W.1    Schulten, K.2
  • 50
    • 0001641777 scopus 로고    scopus 로고
    • Catalysis in human hypoxanthine-guanine phosphoribosyltransferase: Asp-137 acts as a general acid/base
    • Xu Y., Grubmeyer C. Catalysis in human hypoxanthine-guanine phosphoribosyltransferase Asp-137 acts as a general acid/base. Biochemistry. 37:1998;4114-4124
    • (1998) Biochemistry , vol.37 , pp. 4114-4124
    • Xu, Y.1    Grubmeyer, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.