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Volumn 6, Issue 12, 1997, Pages 2504-2511

Crystal structures of a marginally active thymidylate synthase mutant, Arg 126 → Glu

Author keywords

Enzyme mechanism; Inhibitor; Mutation; X ray crystallography

Indexed keywords

10 PROPARGYL 5,8 DIDEAZAFOLIC ACID; ARGININE; BACTERIAL ENZYME; CYSTEINE; DEOXYURIDINE PHOSPHATE; GLUTAMIC ACID; METHYLENETETRAHYDROFOLIC ACID; MUTANT PROTEIN; PHOSPHATE; THYMIDINE PHOSPHATE; THYMIDYLATE SYNTHASE;

EID: 0031452278     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560061203     Document Type: Article
Times cited : (11)

References (31)
  • 1
    • 0000913086 scopus 로고
    • A last algorithm for rendering space-filling molecule pictures
    • Bacon DJ, Anderson WF. 1988. A last algorithm for rendering space-filling molecule pictures. J Mol Graphics 6:219-220.
    • (1988) J Mol Graphics , vol.6 , pp. 219-220
    • Bacon, D.J.1    Anderson, W.F.2
  • 2
    • 0024279342 scopus 로고
    • Crystallographic refinement by simulated annealing. Application to a 2.8 Å resolution structure of aspartate aminotransferase
    • Brunger AT. 1988. Crystallographic refinement by simulated annealing. Application to a 2.8 Å resolution structure of aspartate aminotransferase. J Mol Biol 203:803-816.
    • (1988) J Mol Biol , vol.203 , pp. 803-816
    • Brunger, A.T.1
  • 3
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger AT. 1992. Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355:472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 5
    • 0029036377 scopus 로고
    • The catalytic mechanism and structure of thymidylate synthase
    • Carreras CW, Santi DV. 1995. The catalytic mechanism and structure of thymidylate synthase. Annu Rev Biochem 64:721-762.
    • (1995) Annu Rev Biochem , vol.64 , pp. 721-762
    • Carreras, C.W.1    Santi, D.V.2
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project N. 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D50:760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 8
    • 0028295613 scopus 로고
    • Water-mediated substrate/product discrimination: The product complex of thymidylate synthase at 1.83 Å
    • Fauman EB, Rutenber EE, Maley GF, Maley F, Stroud RM. 1994. Water-mediated substrate/product discrimination: The product complex of thymidylate synthase at 1.83 Å. Biochemistry 33:1502-1511.
    • (1994) Biochemistry , vol.33 , pp. 1502-1511
    • Fauman, E.B.1    Rutenber, E.E.2    Maley, G.F.3    Maley, F.4    Stroud, R.M.5
  • 9
    • 0025295135 scopus 로고
    • Pairwise specificity and sequential binding in enzyme catalysis: Thymidylate synthase
    • Finer-Moore JS, Montfort WR, Stroud RM. 1990. Pairwise specificity and sequential binding in enzyme catalysis: Thymidylate synthase. Biochemistry 29:6977-6986.
    • (1990) Biochemistry , vol.29 , pp. 6977-6986
    • Finer-Moore, J.S.1    Montfort, W.R.2    Stroud, R.M.3
  • 10
    • 0029433529 scopus 로고
    • Structural aspects of the inhibition and catalytic mechanism of thymidylate synthase
    • Hardy LW. 1995. Structural aspects of the inhibition and catalytic mechanism of thymidylate synthase. Acta Biochim Polon 42:367-380.
    • (1995) Acta Biochim Polon , vol.42 , pp. 367-380
    • Hardy, L.W.1
  • 11
    • 0030991713 scopus 로고    scopus 로고
    • Use of strain in a stereospecific catalytic mechanism: Crystal structures of Escherichia coli thymidylate synthase bound to FdUMP and methylenetetrahydrofolate
    • Hyatt DC, Maley F, Montfort WR. 1997. Use of strain in a stereospecific catalytic mechanism: Crystal structures of Escherichia coli thymidylate synthase bound to FdUMP and methylenetetrahydrofolate. Biochemistry 36:4585-4594.
    • (1997) Biochemistry , vol.36 , pp. 4585-4594
    • Hyatt, D.C.1    Maley, F.2    Montfort, W.R.3
  • 12
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjelgard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A47:110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjelgard, M.4
  • 13
    • 0019368721 scopus 로고
    • A potent antitumor quinazoline inhibitor of thymidylate synthetase: Synthesis, biological properties, and therapeutic results in mice
    • Jones TR, Calvert AH, Jackman AL, Brown SJ, Jones M, Harrap KR. 1981. A potent antitumor quinazoline inhibitor of thymidylate synthetase: Synthesis, biological properties, and therapeutic results in mice. Eur J Cancer 17:11-19.
    • (1981) Eur J Cancer , vol.17 , pp. 11-19
    • Jones, T.R.1    Calvert, A.H.2    Jackman, A.L.3    Brown, S.J.4    Jones, M.5    Harrap, K.R.6
  • 14
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch W. 1988. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J Appl Crystallogr 21:916-934.
    • (1988) J Appl Crystallogr , vol.21 , pp. 916-934
    • Kabsch, W.1
  • 15
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 16
    • 0019171347 scopus 로고
    • Hydrodynamic behavior of human and bacterial thymidylate synthetases and thymidylate synthetase-5-fluoro-2′deoxyuridylate-5,10-methylenetetrahydrofolate complexes. Evidence for large conformational changes during catalysis
    • Lockshin A, Danenberg PV. 1980. Hydrodynamic behavior of human and bacterial thymidylate synthetases and thymidylate synthetase-5-fluoro-2′deoxyuridylate-5,10-methylenetetrahydrofolate complexes. Evidence for large conformational changes during catalysis. Biochemistry 19:4244-4251.
    • (1980) Biochemistry , vol.19 , pp. 4244-4251
    • Lockshin, A.1    Danenberg, P.V.2
  • 17
    • 0028961319 scopus 로고
    • Complete restoration of activity to inactive mutants of Escherichia coli thymidylate synthase: Evidence that E. coli thymidylate synthase is a half-the-sites activity enzyme
    • Maley F, Pedersen-Lane J, Changchien L. 1995. Complete restoration of activity to inactive mutants of Escherichia coli thymidylate synthase: Evidence that E. coli thymidylate synthase is a half-the-sites activity enzyme. Biochemistry 34:1469-1474.
    • (1995) Biochemistry , vol.34 , pp. 1469-1474
    • Maley, F.1    Pedersen-Lane, J.2    Changchien, L.3
  • 18
    • 0024278707 scopus 로고
    • Properties of a defined mutant of Escherichia coli thymidylate synthase
    • Maley GF, Maley F. 1988. Properties of a defined mutant of Escherichia coli thymidylate synthase. J Biol Chem 263:7620-7627.
    • (1988) J Biol Chem , vol.263 , pp. 7620-7627
    • Maley, G.F.1    Maley, F.2
  • 19
    • 0025149019 scopus 로고
    • Crystal structure of Escherichia coli thymidylate synthase containing bound 5-fluoro-2′-deoxyuridylate and 10-propargyl-5,8-dideazafolate
    • Matthews DA, Appelt K, Oatley SJ, Xuong NH. 1990a. Crystal structure of Escherichia coli thymidylate synthase containing bound 5-fluoro-2′-deoxyuridylate and 10-propargyl-5,8-dideazafolate. J Mol Biol 214:923-936.
    • (1990) J Mol Biol , vol.214 , pp. 923-936
    • Matthews, D.A.1    Appelt, K.2    Oatley, S.J.3    Xuong, N.H.4
  • 20
    • 0025091668 scopus 로고
    • Stereochemical mechanism of action for thymidylate synthase based on the X-ray structure of the covalent inhibitor ternary complex with 5-fluoro-2′-deoxyuridylate and 5,10-methylenetetrahydrofolate
    • Matthews DA, Villafranca JE, Janson CA, Smith WW, Welsh K, Freer S. 1990b. Stereochemical mechanism of action for thymidylate synthase based on the X-ray structure of the covalent inhibitor ternary complex with 5-fluoro-2′-deoxyuridylate and 5,10-methylenetetrahydrofolate. J Mol Biol 214:937-948.
    • (1990) J Mol Biol , vol.214 , pp. 937-948
    • Matthews, D.A.1    Villafranca, J.E.2    Janson, C.A.3    Smith, W.W.4    Welsh, K.5    Freer, S.6
  • 21
    • 0028057108 scopus 로고
    • Raster3D version 2.0 - A program for photorealistic molecular graphics
    • Merritt EA, Murphy MEP. 1994. Raster3D version 2.0 - A program for photorealistic molecular graphics. Acta Crystallogr D50:869-873.
    • (1994) Acta Crystallogr , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 22
    • 85027633237 scopus 로고
    • Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography
    • Messerschmidt A, Pflugrath JW. 1987. Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography. J Appl Crystallogr 20:306-315.
    • (1987) J Appl Crystallogr , vol.20 , pp. 306-315
    • Messerschmidt, A.1    Pflugrath, J.W.2
  • 23
    • 0025372246 scopus 로고
    • Escherichia coli thymidylate synthase: Amino acid substitutions by suppression of amber non-sense mutations
    • Michaels ML, Kim CW, Matthews DA, Miller JH. 1990. Escherichia coli thymidylate synthase: Amino acid substitutions by suppression of amber non-sense mutations. Proc Natl Acad Sci USA 87:3957-3961.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3957-3961
    • Michaels, M.L.1    Kim, C.W.2    Matthews, D.A.3    Miller, J.H.4
  • 26
    • 0022518273 scopus 로고
    • Kinetics and mechanism of interaction of 10-propargyl-5,8-dideazafolate with thymidylate synthase
    • Pogolotti AL Jr, Danenberg PV, Santi DV. 1986. Kinetics and mechanism of interaction of 10-propargyl-5,8-dideazafolate with thymidylate synthase. J Med Chem 29:478-482.
    • (1986) J Med Chem , vol.29 , pp. 478-482
    • Pogolotti Jr., A.L.1    Danenberg, P.V.2    Santi, D.V.3
  • 27
    • 0030466872 scopus 로고    scopus 로고
    • An essential role for water in an enzyme reaction mechanism: The crystal structure of the thymidylate synthase mutant E58Q
    • Sage CR, Rutenber EE, Stout TJ, Stroud RM. 1996. An essential role for water in an enzyme reaction mechanism: The crystal structure of the thymidylate synthase mutant E58Q. Biochemistry 35:16270-16281.
    • (1996) Biochemistry , vol.35 , pp. 16270-16281
    • Sage, C.R.1    Rutenber, E.E.2    Stout, T.J.3    Stroud, R.M.4
  • 28
    • 0025234376 scopus 로고
    • Site-directed mutagenesis of arginine 179 of thymidylate synthase. A nonessential substrate-binding residue
    • Santi DV, Pinter K, Kealey J, Davisson VJ. 1990. Site-directed mutagenesis of arginine 179 of thymidylate synthase. A nonessential substrate-binding residue. J Biol Chem 265:6770-6775.
    • (1990) J Biol Chem , vol.265 , pp. 6770-6775
    • Santi, D.V.1    Pinter, K.2    Kealey, J.3    Davisson, V.J.4
  • 29
    • 84913050729 scopus 로고
    • General purpose least-squares refinement program for macromolecular structures
    • Tronrud DE, Ten Eyck LF, Matthews BW. 1987. General purpose least-squares refinement program for macromolecular structures. Acta Crystallogr A43:489-501.
    • (1987) Acta Crystallogr , vol.A43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 30
    • 0001530879 scopus 로고
    • Direct spectrophotometric evidence for oxidation of tetrahydrofolate during enzymatic synthesis of thymidylate
    • Wahba AJ, Friedkin M. 1962. Direct spectrophotometric evidence for oxidation of tetrahydrofolate during enzymatic synthesis of thymidylate. J Biol Chem 237:3794-3801.
    • (1962) J Biol Chem , vol.237 , pp. 3794-3801
    • Wahba, A.J.1    Friedkin, M.2
  • 31
    • 0002863521 scopus 로고
    • Strategies for extracting isomorphous and anomalous signals
    • Sayre, D., ed. Oxford: Clarendon Press
    • Weissman L. 1982. Strategies for extracting isomorphous and anomalous signals. In: Sayre, D., ed. Computational crystallography. Oxford: Clarendon Press. pp 56-63.
    • (1982) Computational Crystallography , pp. 56-63
    • Weissman, L.1


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