메뉴 건너뛰기




Volumn 373, Issue 1, 2007, Pages 48-64

The Crystal Structure of the Bifunctional Deaminase/Reductase RibD of the Riboflavin Biosynthetic Pathway in Escherichia coli: Implications for the Reductive Mechanism

Author keywords

3D structure comparison; bi functional deaminase reductase; hydride transfer; NADPH; riboflavin biosynthesis

Indexed keywords

BACTERIAL ENZYME; DEAMINASE; DIHYDROFOLATE REDUCTASE; OXIDOREDUCTASE; PROTEIN RIBD; RIBOFLAVIN; UNCLASSIFIED DRUG;

EID: 34548548871     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.12.009     Document Type: Article
Times cited : (23)

References (68)
  • 2
    • 0037100667 scopus 로고    scopus 로고
    • Regulation of riboflavin biosynthesis and transport genes in bacteria by transcriptional and translational attenuation
    • Vitreschak A.G., Rodionov D.A., Mironov A.A., and Gelfand M.S. Regulation of riboflavin biosynthesis and transport genes in bacteria by transcriptional and translational attenuation. Nucl. Acids Res. 30 (2002) 3141-3151
    • (2002) Nucl. Acids Res. , vol.30 , pp. 3141-3151
    • Vitreschak, A.G.1    Rodionov, D.A.2    Mironov, A.A.3    Gelfand, M.S.4
  • 3
    • 0001302597 scopus 로고    scopus 로고
    • Inactivation of the ypaA gene in Bacillus subtilis; analysis of the resulting phenotypic expression Russ
    • Kreneva R.A., Gelfand M.S., Mironov A.A., Yomantas Y.A.I.K.Y., Mironov A.S., and Perumov D.A. Inactivation of the ypaA gene in Bacillus subtilis; analysis of the resulting phenotypic expression Russ. J. Genet. 36 (2000) 972-974
    • (2000) J. Genet. , vol.36 , pp. 972-974
    • Kreneva, R.A.1    Gelfand, M.S.2    Mironov, A.A.3    Yomantas, Y.A.I.K.Y.4    Mironov, A.S.5    Perumov, D.A.6
  • 4
    • 0036334571 scopus 로고    scopus 로고
    • From genetic footprinting to antimicrobial drug targets: examples in cofactor biosynthetic pathways
    • Gerdes S.Y., Scholle M.D., D'Souza M., Bernal A., Baev M.V., Farrell M., et al. From genetic footprinting to antimicrobial drug targets: examples in cofactor biosynthetic pathways. J. Bacteriol. 184 (2002) 4555-4572
    • (2002) J. Bacteriol. , vol.184 , pp. 4555-4572
    • Gerdes, S.Y.1    Scholle, M.D.2    D'Souza, M.3    Bernal, A.4    Baev, M.V.5    Farrell, M.6
  • 6
    • 0030946770 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin: characterization of the bifunctional deaminase-reductase of Escherichia coli and Bacillus subtilis
    • Richter G., Fischer M., Krieger C., Eberhardt S., Luttgen H., Gerstenschlager I., and Bacher A. Biosynthesis of riboflavin: characterization of the bifunctional deaminase-reductase of Escherichia coli and Bacillus subtilis. J. Bacteriol. 179 (1997) 2022-2028
    • (1997) J. Bacteriol. , vol.179 , pp. 2022-2028
    • Richter, G.1    Fischer, M.2    Krieger, C.3    Eberhardt, S.4    Luttgen, H.5    Gerstenschlager, I.6    Bacher, A.7
  • 7
    • 0018087061 scopus 로고
    • Presence of Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin
    • Burrows R.B., and Brown G.M. Presence of Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin. J. Bacteriol. 136 (1978) 657-667
    • (1978) J. Bacteriol. , vol.136 , pp. 657-667
    • Burrows, R.B.1    Brown, G.M.2
  • 8
    • 0018802668 scopus 로고
    • Biosynthesis of riboflavin: reductase and deaminase of Ashbya gossypii
    • Hollander I., and Brown G.M. Biosynthesis of riboflavin: reductase and deaminase of Ashbya gossypii. Biochem. Biophys. Res. Commun. 89 (1979) 759-763
    • (1979) Biochem. Biophys. Res. Commun. , vol.89 , pp. 759-763
    • Hollander, I.1    Brown, G.M.2
  • 9
    • 0019807080 scopus 로고
    • Biosynthesis of riboflavin. Characterization of the product of the deaminase
    • Nielsen P., and Bacher A. Biosynthesis of riboflavin. Characterization of the product of the deaminase. Biochim. Biophys. Acta 662 (1981) 312-317
    • (1981) Biochim. Biophys. Acta , vol.662 , pp. 312-317
    • Nielsen, P.1    Bacher, A.2
  • 10
    • 0015351687 scopus 로고
    • Biosynthesis of riboflavine in Saccharomyces cerevisiae: the role of genes rib 1 and rib 7
    • Oltmanns O., and Bacher A. Biosynthesis of riboflavine in Saccharomyces cerevisiae: the role of genes rib 1 and rib 7. J. Bacteriol. 110 (1972) 818-822
    • (1972) J. Bacteriol. , vol.110 , pp. 818-822
    • Oltmanns, O.1    Bacher, A.2
  • 11
    • 4344648767 scopus 로고    scopus 로고
    • Evolution of vitamin B2 biosynthesis: structural and functional similarity between pyrimidine deaminases of eubacterial and plant origin
    • Fischer M., Romisch W., Saller S., Illarionov B., Richter G., Rohdich F., et al. Evolution of vitamin B2 biosynthesis: structural and functional similarity between pyrimidine deaminases of eubacterial and plant origin. J. Biol. Chem. 279 (2004) 36299-36308
    • (2004) J. Biol. Chem. , vol.279 , pp. 36299-36308
    • Fischer, M.1    Romisch, W.2    Saller, S.3    Illarionov, B.4    Richter, G.5    Rohdich, F.6
  • 12
    • 0036203061 scopus 로고    scopus 로고
    • The pyrimidine nucleotide reductase step in riboflavin and F(420) biosynthesis in archaea proceeds by the eukaryotic route to riboflavin
    • Graupner M., Xu H., and White R.H. The pyrimidine nucleotide reductase step in riboflavin and F(420) biosynthesis in archaea proceeds by the eukaryotic route to riboflavin. J. Bacteriol. 184 (2002) 1952-1957
    • (2002) J. Bacteriol. , vol.184 , pp. 1952-1957
    • Graupner, M.1    Xu, H.2    White, R.H.3
  • 13
    • 0001890332 scopus 로고
    • Crystal structure, coenzyme conformations, and protein interactions
    • David Dolphin R.P., and Avramovic O. (Eds), John Wiley & Sons Part A
    • Eklund H., and Brändén C.I. Crystal structure, coenzyme conformations, and protein interactions. In: David Dolphin R.P., and Avramovic O. (Eds). Pyridine Nucleotide Coenzymes; Chemical, Biochemical and Medical Aspects (1987), John Wiley & Sons 51-98 Part A
    • (1987) Pyridine Nucleotide Coenzymes; Chemical, Biochemical and Medical Aspects , pp. 51-98
    • Eklund, H.1    Brändén, C.I.2
  • 14
    • 0024295016 scopus 로고
    • Biosynthesis of riboflavin: mechanism of formation of the ribitylamino linkage
    • Keller P.J., Le Van Q., Kim S.U., Bown D.H., Chen H.C., Kohnle A., et al. Biosynthesis of riboflavin: mechanism of formation of the ribitylamino linkage. Biochemistry 27 (1988) 1117-1120
    • (1988) Biochemistry , vol.27 , pp. 1117-1120
    • Keller, P.J.1    Le Van, Q.2    Kim, S.U.3    Bown, D.H.4    Chen, H.C.5    Kohnle, A.6
  • 15
    • 33646365634 scopus 로고    scopus 로고
    • Crystal structure of a bifunctional deaminase and reductase from Bacillus subtilis involved in riboflavin biosynthesis
    • Chen S.C., Chang Y.C., Lin C.H., Lin C.H., and Liaw S.H. Crystal structure of a bifunctional deaminase and reductase from Bacillus subtilis involved in riboflavin biosynthesis. J. Biol. Chem. 281 (2006) 7605-7613
    • (2006) J. Biol. Chem. , vol.281 , pp. 7605-7613
    • Chen, S.C.1    Chang, Y.C.2    Lin, C.H.3    Lin, C.H.4    Liaw, S.H.5
  • 16
    • 33745159681 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin: structure and properties of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5′-phosphate reductase of Methanocaldococcus jannaschii
    • Chatwell L., Krojer T., Fidler A., Romisch W., Eisenreich W., Bacher A., et al. Biosynthesis of riboflavin: structure and properties of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5′-phosphate reductase of Methanocaldococcus jannaschii. J. Mol. Biol. 359 (2006) 1334-1351
    • (2006) J. Mol. Biol. , vol.359 , pp. 1334-1351
    • Chatwell, L.1    Krojer, T.2    Fidler, A.3    Romisch, W.4    Eisenreich, W.5    Bacher, A.6
  • 17
    • 0028961335 scopus 로고
    • SCOP: a structural classification of proteins database for the investigation of sequences and structures
    • Murzin A.G., Brenner S.E., Hubbard T., and Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247 (1995) 536-540
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 18
    • 84944812409 scopus 로고
    • Improved coefficients for map calculation using partial structures with errors
    • Read R.J. Improved coefficients for map calculation using partial structures with errors. Acta Crystallog. sect. A 42 (1986) 140-149
    • (1986) Acta Crystallog. sect. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 19
    • 4644264487 scopus 로고    scopus 로고
    • Evolution of vitamin B2 biosynthesis: a novel class of riboflavin synthase in Archaea
    • Fischer M., Schott A.K., Romisch W., Ramsperger A., Augustin M., Fidler A., et al. Evolution of vitamin B2 biosynthesis: a novel class of riboflavin synthase in Archaea. J. Mol. Biol. 343 (2004) 267-278
    • (2004) J. Mol. Biol. , vol.343 , pp. 267-278
    • Fischer, M.1    Schott, A.K.2    Romisch, W.3    Ramsperger, A.4    Augustin, M.5    Fidler, A.6
  • 20
    • 33646195686 scopus 로고    scopus 로고
    • Berthold M.R., Glen R., Diederichs K., Kohlbacher O., Fischer I., et al. (Eds), Sringer-Verlag, Berlin Heidelberg
    • Krissinel E., and Henrick K. In: Berthold M.R., Glen R., Diederichs K., Kohlbacher O., Fischer I., et al. (Eds). Detection of Protein Assemblies in Crystals. CompLife 2005 vol. 3695 (2005), Sringer-Verlag, Berlin Heidelberg 163-174
    • (2005) Detection of Protein Assemblies in Crystals. CompLife 2005 , vol.3695 , pp. 163-174
    • Krissinel, E.1    Henrick, K.2
  • 21
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22 (1994) 4673-4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 23
    • 0037460985 scopus 로고    scopus 로고
    • TIGR Gene Indices clustering tools (TGICL): a software system for fast clustering of large EST datasets
    • Pertea G., Huang X., Liang F., Antonescu V., Sultana R., Karamycheva S., et al. TIGR Gene Indices clustering tools (TGICL): a software system for fast clustering of large EST datasets. Bioinformatics 19 (2003) 651-652
    • (2003) Bioinformatics , vol.19 , pp. 651-652
    • Pertea, G.1    Huang, X.2    Liang, F.3    Antonescu, V.4    Sultana, R.5    Karamycheva, S.6
  • 24
    • 0033965855 scopus 로고    scopus 로고
    • The TIGR gene indices: reconstruction and representation of expressed gene sequences
    • Quackenbush J., Liang F., Holt I., Pertea G., and Upton J. The TIGR gene indices: reconstruction and representation of expressed gene sequences. Nucl. Acids Res. 28 (2000) 141-145
    • (2000) Nucl. Acids Res. , vol.28 , pp. 141-145
    • Quackenbush, J.1    Liang, F.2    Holt, I.3    Pertea, G.4    Upton, J.5
  • 25
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence
    • Sawaya M.R., and Kraut J. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry 36 (1997) 586-603
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 26
    • 0034737320 scopus 로고    scopus 로고
    • The crystal structure of dihydrofolate reductase from Thermotoga maritima: molecular features of thermostability
    • Dams T., Auerbach G., Bader G., Jacob U., Ploom T., Huber R., and Jaenicke R. The crystal structure of dihydrofolate reductase from Thermotoga maritima: molecular features of thermostability. J. Mol. Biol. 297 (2000) 659-672
    • (2000) J. Mol. Biol. , vol.297 , pp. 659-672
    • Dams, T.1    Auerbach, G.2    Bader, G.3    Jacob, U.4    Ploom, T.5    Huber, R.6    Jaenicke, R.7
  • 27
    • 23944518876 scopus 로고    scopus 로고
    • Structure and hydride transfer mechanism of a moderate thermophilic dihydrofolate reductase from Bacillus stearothermophilus and comparison to its mesophilic and hyperthermophilic homologues
    • Kim H.S., Damo S.M., Lee S.Y., Wemmer D., and Klinman J.P. Structure and hydride transfer mechanism of a moderate thermophilic dihydrofolate reductase from Bacillus stearothermophilus and comparison to its mesophilic and hyperthermophilic homologues. Biochemistry 44 (2005) 11428-11439
    • (2005) Biochemistry , vol.44 , pp. 11428-11439
    • Kim, H.S.1    Damo, S.M.2    Lee, S.Y.3    Wemmer, D.4    Klinman, J.P.5
  • 28
    • 0026065644 scopus 로고
    • Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding
    • Bystroff C., and Kraut J. Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding. Biochemistry 30 (1991) 2227-2239
    • (1991) Biochemistry , vol.30 , pp. 2227-2239
    • Bystroff, C.1    Kraut, J.2
  • 29
    • 0026757079 scopus 로고
    • Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition-state stabilization
    • Li L., Falzone C.J., Wright P.E., and Benkovic S.J. Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition-state stabilization. Biochemistry 31 (1992) 7826-7833
    • (1992) Biochemistry , vol.31 , pp. 7826-7833
    • Li, L.1    Falzone, C.J.2    Wright, P.E.3    Benkovic, S.J.4
  • 31
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • Fierke C.A., Johnson K.A., and Benkovic S.J. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry 26 (1987) 4085-4092
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 32
    • 21444435324 scopus 로고    scopus 로고
    • Understanding the role of Leu22 variants in methotrexate resistance: comparison of wild-type and Leu22Arg variant mouse and human dihydrofolate reductase ternary crystal complexes with methotrexate and NADPH
    • Cody V., Luft J.R., and Pangborn W. Understanding the role of Leu22 variants in methotrexate resistance: comparison of wild-type and Leu22Arg variant mouse and human dihydrofolate reductase ternary crystal complexes with methotrexate and NADPH. Acta Crystallog. sect. D 61 (2005) 147-155
    • (2005) Acta Crystallog. sect. D , vol.61 , pp. 147-155
    • Cody, V.1    Luft, J.R.2    Pangborn, W.3
  • 33
    • 0034645774 scopus 로고    scopus 로고
    • Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs
    • Li R., Sirawaraporn R., Chitnumsub P., Sirawaraporn W., Wooden J., Athappilly F., et al. Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs. J. Mol. Biol. 295 (2000) 307-323
    • (2000) J. Mol. Biol. , vol.295 , pp. 307-323
    • Li, R.1    Sirawaraporn, R.2    Chitnumsub, P.3    Sirawaraporn, W.4    Wooden, J.5    Athappilly, F.6
  • 34
    • 0020441466 scopus 로고
    • Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate
    • Bolin J.T., Filman D.J., Matthews D.A., Hamlin R.C., and Kraut J. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate. J. Biol. Chem. 257 (1982) 13650-13662
    • (1982) J. Biol. Chem. , vol.257 , pp. 13650-13662
    • Bolin, J.T.1    Filman, D.J.2    Matthews, D.A.3    Hamlin, R.C.4    Kraut, J.5
  • 37
    • 0030731508 scopus 로고    scopus 로고
    • X-ray crystallographic studies of Candida albicans dihydrofolate reductase. High resolution structures of the holoenzyme and an inhibited ternary complex
    • Whitlow M., Howard A.J., Stewart D., Hardman K.D., Kuyper L.F., Baccanari D.P., et al. X-ray crystallographic studies of Candida albicans dihydrofolate reductase. High resolution structures of the holoenzyme and an inhibited ternary complex. J. Biol. Chem. 272 (1997) 30289-30298
    • (1997) J. Biol. Chem. , vol.272 , pp. 30289-30298
    • Whitlow, M.1    Howard, A.J.2    Stewart, D.3    Hardman, K.D.4    Kuyper, L.F.5    Baccanari, D.P.6
  • 38
    • 0025805956 scopus 로고
    • Role of the conserved active site residue tryptophan-24 of human dihydrofolate reductase as revealed by mutagenesis
    • Beard W.A., Appleman J.R., Huang S.M., Delcamp T.J., Freisheim J.H., and Blakley R.L. Role of the conserved active site residue tryptophan-24 of human dihydrofolate reductase as revealed by mutagenesis. Biochemistry 30 (1991) 1432-1440
    • (1991) Biochemistry , vol.30 , pp. 1432-1440
    • Beard, W.A.1    Appleman, J.R.2    Huang, S.M.3    Delcamp, T.J.4    Freisheim, J.H.5    Blakley, R.L.6
  • 39
    • 0016594328 scopus 로고
    • 31P NMR studies of NADPH and NADP+ binding to L. casei dihydrofolate reductase
    • Feeney J., Birdsall B., Roberts G.C., and Burgen A.S. 31P NMR studies of NADPH and NADP+ binding to L. casei dihydrofolate reductase. Nature 257 (1975) 564-566
    • (1975) Nature , vol.257 , pp. 564-566
    • Feeney, J.1    Birdsall, B.2    Roberts, G.C.3    Burgen, A.S.4
  • 40
    • 0024990110 scopus 로고
    • Role of lysine-54 in determining cofactor specificity and binding in human dihydrofolate reductase
    • Huang S., Appleman R., Tan X.H., Thompson P.D., Blakley R.L., Sheridan R.P., et al. Role of lysine-54 in determining cofactor specificity and binding in human dihydrofolate reductase. Biochemistry 29 (1990) 8063-8069
    • (1990) Biochemistry , vol.29 , pp. 8063-8069
    • Huang, S.1    Appleman, R.2    Tan, X.H.3    Thompson, P.D.4    Blakley, R.L.5    Sheridan, R.P.6
  • 41
    • 0018399517 scopus 로고
    • Dihydrofolate reductase from Lactobacillus casei. Stereochemistry of NADPH binding
    • Matthews D.A., Alden R.A., Freer S.T., Xuong N., and Kraut J. Dihydrofolate reductase from Lactobacillus casei. Stereochemistry of NADPH binding. J. Biol. Chem. 254 (1979) 4144-4151
    • (1979) J. Biol. Chem. , vol.254 , pp. 4144-4151
    • Matthews, D.A.1    Alden, R.A.2    Freer, S.T.3    Xuong, N.4    Kraut, J.5
  • 42
    • 0025270551 scopus 로고
    • Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state
    • Bystroff C., Oatley S.J., and Kraut J. Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state. Biochemistry 29 (1990) 3263-3277
    • (1990) Biochemistry , vol.29 , pp. 3263-3277
    • Bystroff, C.1    Oatley, S.J.2    Kraut, J.3
  • 43
    • 0033528719 scopus 로고    scopus 로고
    • Ligand-induced conformational changes in the crystal structures of Pneumocystis carinii dihydrofolate reductase complexes with folate and NADP+
    • Cody V., Galitsky N., Rak D., Luft J.R., Pangborn W., and Queener S.F. Ligand-induced conformational changes in the crystal structures of Pneumocystis carinii dihydrofolate reductase complexes with folate and NADP+. Biochemistry 38 (1999) 4303-4312
    • (1999) Biochemistry , vol.38 , pp. 4303-4312
    • Cody, V.1    Galitsky, N.2    Rak, D.3    Luft, J.R.4    Pangborn, W.5    Queener, S.F.6
  • 45
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., and Clardy J. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229 (1993) 105-124
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 46
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 26 (1993) 795-800
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 47
    • 0027432378 scopus 로고
    • Conformational analysis of human dihydrofolate reductase inhibitor complexes: crystal structure determination of wild type and F31 mutant binary and ternary inhibitor complexes
    • Cody V., Wojtczak A., Kalman T.I., Friesheim J.H., and Blakley R.L. Conformational analysis of human dihydrofolate reductase inhibitor complexes: crystal structure determination of wild type and F31 mutant binary and ternary inhibitor complexes. Advan. Exp. Med. Biol. 338 (1993) 481-486
    • (1993) Advan. Exp. Med. Biol. , vol.338 , pp. 481-486
    • Cody, V.1    Wojtczak, A.2    Kalman, T.I.3    Friesheim, J.H.4    Blakley, R.L.5
  • 48
    • 0030785537 scopus 로고    scopus 로고
    • Comparison of ternary complexes of Pneumocystis carinii and wild-type human dihydrofolate reductase with coenzyme NADPH and a novel classical antitumor furo [2,3-d]pyrimidine antifolate
    • Cody V., Galitsky N., Luft J.R., Pangborn W., Gangjee A., Devraj R., et al. Comparison of ternary complexes of Pneumocystis carinii and wild-type human dihydrofolate reductase with coenzyme NADPH and a novel classical antitumor furo [2,3-d]pyrimidine antifolate. Acta Crystallog. sect. D 53 (1997) 638-649
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 638-649
    • Cody, V.1    Galitsky, N.2    Luft, J.R.3    Pangborn, W.4    Gangjee, A.5    Devraj, R.6
  • 49
    • 0030656217 scopus 로고    scopus 로고
    • Comparison of two independent crystal structures of human dihydrofolate reductase ternary complexes reduced with nicotinamide adenine dinucleotide phosphate and the very tight-binding inhibitor PT523
    • Cody V., Galitsky N., Luft J.R., Pangborn W., Rosowsky A., and Blakley R.L. Comparison of two independent crystal structures of human dihydrofolate reductase ternary complexes reduced with nicotinamide adenine dinucleotide phosphate and the very tight-binding inhibitor PT523. Biochemistry 36 (1997) 13897-13903
    • (1997) Biochemistry , vol.36 , pp. 13897-13903
    • Cody, V.1    Galitsky, N.2    Luft, J.R.3    Pangborn, W.4    Rosowsky, A.5    Blakley, R.L.6
  • 50
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • CCP4. 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
  • 52
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A.A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallog. (1997) 1022-1025
    • (1997) J. Appl. Crystallog. , pp. 1022-1025
    • Vagin, A.A.1    Teplyakov, A.2
  • 53
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 54
  • 55
    • 0000496875 scopus 로고
    • Crystallographic fast Fourier transforms
    • Ten Eyck L.F. Crystallographic fast Fourier transforms. Acta Crystallog. sect. A 29 (1973) 183-191
    • (1973) Acta Crystallog. sect. A , vol.29 , pp. 183-191
    • Ten Eyck, L.F.1
  • 57
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., and Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallog. sect. D 57 (2001) 122-133
    • (2001) Acta Crystallog. sect. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 58
    • 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., and 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
  • 59
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 60
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R.A., Moss D.S., and 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
  • 63
    • 0030332666 scopus 로고    scopus 로고
    • Discovering empirically conserved amino acid substitution groups in databases of protein families
    • Wu T.D., and Brutlag D.L. Discovering empirically conserved amino acid substitution groups in databases of protein families. Proc. Int. Conf. Intell. Syst. Mol. Biol. 4 (1996) 230-240
    • (1996) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.4 , pp. 230-240
    • Wu, T.D.1    Brutlag, D.L.2
  • 64
    • 0028871926 scopus 로고
    • Dali: a network tool for protein structure comparison
    • Holm L., and Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20 (1995) 478-480
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 65
    • 0034479757 scopus 로고    scopus 로고
    • TOP: an automated tool for protein structure comparisons and similarity searches
    • Lu G. TOP: an automated tool for protein structure comparisons and similarity searches. J. Appl. Crystallog. 33 (2000) 176-183
    • (2000) J. Appl. Crystallog. , vol.33 , pp. 176-183
    • Lu, G.1
  • 66
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., and Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallog. sect. D 60 (2004) 2256-2268
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 68
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet P., Robert X., and Courcelle E. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucl. Acids Res. 31 (2003) 3320-3323
    • (2003) Nucl. Acids Res. , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.