메뉴 건너뛰기




Volumn 7, Issue 5, 1999, Pages 583-595

The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 Å resolution reveals a novel fold

Author keywords

Four layer sandwich; Gene duplication; MAD phasing; Pyruvoyl dependent enzymes; S adenosylmethionine decarboxylase

Indexed keywords

ADENOSYLMETHIONINE DECARBOXYLASE;

EID: 0033134691     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80074-4     Document Type: Article
Times cited : (70)

References (50)
  • 1
    • 0027097783 scopus 로고
    • S-adenosylmethionine decarboxylase as an enzyme target for therapy
    • Pegg, A.E. & McCann, P.P. (1992). S-adenosylmethionine decarboxylase as an enzyme target for therapy. Pharmacol. Ther. 56, 359-377.
    • (1992) Pharmacol. Ther. , vol.56 , pp. 359-377
    • Pegg, A.E.1    McCann, P.P.2
  • 3
    • 0002950121 scopus 로고
    • S-adenosylmethionine decarboxylase regulation and processing
    • (Robert A. Casero, Jr., ed.), R.G. Landes Co., Georgetown, TX
    • Stanley, B.A. (1995). S-adenosylmethionine decarboxylase regulation and processing. In Polyamines: Regulation and Molecular Interaction. (Robert A. Casero, Jr., ed.), pp. 27-75, R.G. Landes Co., Georgetown, TX.
    • (1995) Polyamines: Regulation and Molecular Interaction , pp. 27-75
    • Stanley, B.A.1
  • 4
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy
    • Pegg, A.E. (1988). Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy. Cancer Res. 48, 759-774.
    • (1988) Cancer Res. , vol.48 , pp. 759-774
    • Pegg, A.E.1
  • 6
    • 0000757466 scopus 로고    scopus 로고
    • Pyruvoyl-dependent enzymes
    • (Sinnot, M.L., ed.), Academic Press, Orlando, FL
    • Hackert, M.L. & Pegg, A.E. (1997). Pyruvoyl-dependent enzymes. In Comprehensive Biological Catalysis, Vol. 2. (Sinnot, M.L., ed.), pp. 201-216, Academic Press, Orlando, FL.
    • (1997) Comprehensive Biological Catalysis , vol.2 , pp. 201-216
    • Hackert, M.L.1    Pegg, A.E.2
  • 7
    • 0023109595 scopus 로고
    • Effect of putrescine on the synthesis of S-adenosylmethionine decarboxylase
    • Kameji, T. & Pegg, A.E. (1987). Effect of putrescine on the synthesis of S-adenosylmethionine decarboxylase. Biochem. J. 243, 285-288.
    • (1987) Biochem. J. , vol.243 , pp. 285-288
    • Kameji, T.1    Pegg, A.E.2
  • 8
    • 0028309730 scopus 로고
    • Expression of mammalian S-adenosylmethionine decarboxylase in Escherichia coli: Determination of sites for putrescine activation of activity and processing
    • Stanley, B.A., Shantz, L.M. & Pegg, A.E. (1994). Expression of mammalian S-adenosylmethionine decarboxylase in Escherichia coli: Determination of sites for putrescine activation of activity and processing. J. Biol. Chem. 269, 7901-7907.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7901-7907
    • Stanley, B.A.1    Shantz, L.M.2    Pegg, A.E.3
  • 9
    • 0026684203 scopus 로고
    • Purification of human s-adenosylmethionine decarboxylase expressed in E. Coli and use of this protein to investigate the mechanism of inhibition by the irreversible inhibitors, 5′-deoxy-5′-[(3 hydrazinopropyl)methylamino]adenosine and 5′-{[(z)-4-amino-2- Butenyl]methylamino-5′-deoxyadenosine
    • Shantz, L.M., Stanley, B.A., Secrist, J.A. & Pegg, A.E. (1992). Purification of human s-adenosylmethionine decarboxylase expressed in E. Coli and use of this protein to investigate the mechanism of inhibition by the irreversible inhibitors, 5′-deoxy-5′-[(3 hydrazinopropyl)methylamino]adenosine and 5′-{[(z)-4-amino-2- Butenyl]methylamino)-5′-deoxyadenosine. Biochemistry 31, 6848-6855.
    • (1992) Biochemistry , vol.31 , pp. 6848-6855
    • Shantz, L.M.1    Stanley, B.A.2    Secrist, J.A.3    Pegg, A.E.4
  • 10
    • 0025687384 scopus 로고
    • Spermidine biosynthesis in Saccharomyces cerevisiae: Biosynthesis and processing of a proenzyme form of S-adenosylmethionine decarboxylase
    • Kashiwagi, K., Tanega, S.K., Liu, T. Y., Tabor, C.W. & Tabor, H. (1990). Spermidine biosynthesis in Saccharomyces cerevisiae: Biosynthesis and processing of a proenzyme form of S-adenosylmethionine decarboxylase. J. Biol. Chem. 265, 22321-22328 .
    • (1990) J. Biol. Chem. , vol.265 , pp. 22321-22328
    • Kashiwagi, K.1    Tanega, S.K.2    Liu, T.Y.3    Tabor, C.W.4    Tabor, H.5
  • 11
    • 0024150294 scopus 로고
    • Structural and mechanistic properties of E. Coli S-adenosylmethionine decarboxylase
    • Anton, D.L. & Kutny, R. (1988). Structural and mechanistic properties of E. Coli S-adenosylmethionine decarboxylase. Adv. Exp. Med. Biol. 250, 81-89.
    • (1988) Adv. Exp. Med. Biol. , vol.250 , pp. 81-89
    • Anton, D.L.1    Kutny, R.2
  • 12
    • 0018391720 scopus 로고
    • Investigation of the turnover of rat liver S- adenosylmethionine decarboxylase using a specific antibody
    • Pegg, A.E. (1979). Investigation of the turnover of rat liver S- adenosylmethionine decarboxylase using a specific antibody. J. Biol. Chem. 254, 3249-3253.
    • (1979) J. Biol. Chem. , vol.254 , pp. 3249-3253
    • Pegg, A.E.1
  • 13
    • 0031045715 scopus 로고    scopus 로고
    • CGP48664, a potent and specific S-adenosylmethionine decarboxylase inhibitor: Effects on regulation and stability of the enzyme
    • Svensson, F., Mett, H. & Persson, L. (1997). CGP48664, a potent and specific S-adenosylmethionine decarboxylase inhibitor: Effects on regulation and stability of the enzyme. Biochem. J. 322, 297-302.
    • (1997) Biochem. J. , vol.322 , pp. 297-302
    • Svensson, F.1    Mett, H.2    Persson, L.3
  • 14
    • 0023796129 scopus 로고
    • Structure and regulation of mammalian S-adenosylmethionine decarboxylase
    • Pajunen, A., Pegg, A.E. & et al., (1988). Structure and regulation of mammalian S-adenosylmethionine decarboxylase. J. Biol. Chem. 263, 17040-17049.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17040-17049
    • Pajunen, A.1    Pegg, A.E.2
  • 15
    • 0031947190 scopus 로고
    • Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength
    • Turner, M.A., Yuan, C.S., Borchardt, R.T., Hershfield, M.S., Smith, G.D. & Howell, P.L. (1988). Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength. Nat. Struct. Biol. 5, 369-376.
    • (1988) Nat. Struct. Biol. , vol.5 , pp. 369-376
    • Turner, M.A.1    Yuan, C.S.2    Borchardt, R.T.3    Hershfield, M.S.4    Smith, G.D.5    Howell, P.L.6
  • 19
    • 80055004570 scopus 로고
    • Generalized method of determining heavy-atom positions using the difference Patterson function
    • Terwilliger, T.C., Kim, S.-H. & Eisenberg, D. (1987). Generalized method of determining heavy-atom positions using the difference Patterson function. Acta Crystallogr. A 43, 1-5.
    • (1987) Acta Crystallogr. A , vol.43 , pp. 1-5
    • Terwilliger, T.C.1    Kim, S.-H.2    Eisenberg, D.3
  • 20
    • 0024219852 scopus 로고
    • Crystallographic structure analysis of lamprey hemoglobin from anomalous dispersion of synchrotron radiation
    • Hendrickson, W.A., Smith, J.A., Phizackerley, R.P. & Merritt, E.A. (1988). Crystallographic structure analysis of lamprey hemoglobin from anomalous dispersion of synchrotron radiation. Proteins 4, 77-78.
    • (1988) Proteins , vol.4 , pp. 77-78
    • Hendrickson, W.A.1    Smith, J.A.2    Phizackerley, R.P.3    Merritt, E.A.4
  • 21
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W.A. (1991). Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 22
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • (Wolf, W., Evans, P.R. & Leslie, A.G.W., eds), SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1991). Maximum likelihood refinement of heavy atom parameters. In Proceedings of the CCP4 Study Weekend (Wolf, W., Evans, P.R. & Leslie, A.G.W., eds), pp. 80-88, SERC Daresbury Laboratory, Warrington, UK.
    • (1991) Proceedings of the CCP4 Study Weekend , pp. 80-88
    • Otwinowski, Z.1
  • 23
    • 0028232955 scopus 로고
    • Searching protein structure databases has come of age
    • Holm, L. & Sander, C. (1994). Searching protein structure databases has come of age. Proteins 19, 165-173.
    • (1994) Proteins , vol.19 , pp. 165-173
    • Holm, L.1    Sander, C.2
  • 24
    • 0022382113 scopus 로고
    • Structure determination of histidine decarboxylase from Lactobacillus 30a at 3.0 Å resolution
    • Parks, E.H., Ernst, S.R., Hamlin, R., Xuong, N.H. & Hackert, M.L. (1985). Structure determination of histidine decarboxylase from Lactobacillus 30a at 3.0 Å resolution. J. Mol. Biol. 182, 455-465.
    • (1985) J. Mol. Biol. , vol.182 , pp. 455-465
    • Parks, E.H.1    Ernst, S.R.2    Hamlin, R.3    Xuong, N.H.4    Hackert, M.L.5
  • 25
    • 0024393413 scopus 로고
    • Pyruvoyl-dependent histidine decarboxylase: Active site structure and mechanistic analysis
    • Gallagher, T., Snell, E.E. & Hackert, M.L. (1989). Pyruvoyl-dependent histidine decarboxylase: Active site structure and mechanistic analysis. J. Biol. Chem. 264, 12737-12743.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12737-12743
    • Gallagher, T.1    Snell, E.E.2    Hackert, M.L.3
  • 26
    • 0027276877 scopus 로고
    • Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a
    • Gallagher, T., Rozwarski, D.A., Ernst, S.R. & Hackert, M.L. (1993). Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a. J. Mol. Biol. 230, 516-528.
    • (1993) J. Mol. Biol. , vol.230 , pp. 516-528
    • Gallagher, T.1    Rozwarski, D.A.2    Ernst, S.R.3    Hackert, M.L.4
  • 27
    • 0031960010 scopus 로고    scopus 로고
    • Crystal structure of aspartate decarboxylase at 2.2 Å resolution provides evidence for an ester in protein self-processing
    • Albert, A., Abell, C. & et al., (1998). Crystal structure of aspartate decarboxylase at 2.2 Å resolution provides evidence for an ester in protein self-processing. Nat. Struct. Biol. 5, 289-293.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 289-293
    • Albert, A.1    Abell, C.2
  • 30
    • 0021912751 scopus 로고
    • Pyruvoyl-dependent histidine decarboxylases: Mechanism of cleavage of the proenzyme from Lactobacillus buchneri
    • Recsei, P.A. & Snell, E.E. (1985). Pyruvoyl-dependent histidine decarboxylases: Mechanism of cleavage of the proenzyme from Lactobacillus buchneri. J. Biol. Chem. 260, 2804-2806.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2804-2806
    • Recsei, P.A.1    Snell, E.E.2
  • 31
    • 0026015245 scopus 로고
    • Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity
    • Stanley, B.A. & Pegg, A.E. (1991). Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity. J. Biol. Chem. 266, 18502-18506.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18502-18506
    • Stanley, B.A.1    Pegg, A.E.2
  • 33
  • 34
    • 0030695934 scopus 로고    scopus 로고
    • Processing of mammalian and plant S-adenosylmethionine decarboxylase proenzymes
    • Xiong, H., Stanley, B.A., Tekwani, B.L. & Pegg, A.E. (1997). Processing of mammalian and plant S-adenosylmethionine decarboxylase proenzymes. J. Biol. Chem. 272, 28342-28348.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28342-28348
    • Xiong, H.1    Stanley, B.A.2    Tekwani, B.L.3    Pegg, A.E.4
  • 35
    • 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, 409-411.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.H.2
  • 36
    • 0031059866 scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. (1991). Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1991) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1
  • 37
    • 84944813643 scopus 로고
    • On the application of phase relationships to complex structures. XXII. Techniques for random phase refinement
    • Debaerdemaeker, T. & Woolfson, M.M. (1983). On the application of phase relationships to complex structures. XXII. Techniques for random phase refinement. Acta Crystallogr. A 39, 193-196.
    • (1983) Acta Crystallogr. A , vol.39 , pp. 193-196
    • Debaerdemaeker, T.1    Woolfson, M.M.2
  • 38
    • 0001804798 scopus 로고
    • A minimal principle in the phase problem
    • (Moras, D., Podarny, A.D. & Thierry, J.C., eds), IUCr Oxford University Press, Oxford, UK
    • Hauptman, H.A. (1991). A minimal principle in the phase problem. In Crystallographic Computing 5: From Chemistry to Biology. (Moras, D., Podarny, A.D. & Thierry, J.C., eds), pp. 324-332, IUCr Oxford University Press, Oxford, UK.
    • (1991) Crystallographic Computing 5: from Chemistry to Biology , pp. 324-332
    • Hauptman, H.A.1
  • 39
    • 85030359841 scopus 로고
    • ACA meeting abstract
    • Hauptman, H.A. (1988). ACA meeting abstract.
    • (1988)
    • Hauptman, H.A.1
  • 40
    • 0001431519 scopus 로고
    • DREADD - Data reduction and error analysis for single crystal diffractometer data
    • Blessing, R.H. (1989). DREADD - Data reduction and error analysis for single crystal diffractometer data. J. Appl. Crystallogr. 22, 396-397.
    • (1989) J. Appl. Crystallogr. , vol.22 , pp. 396-397
    • Blessing, R.H.1
  • 42
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjelgaard, M. (1991). Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjelgaard, M.4
  • 44
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quality for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). The free R value: A novel statistical quality for assessing the accuracy of crystal structures. Nature 335, 472-474.
    • (1992) Nature , vol.335 , pp. 472-474
    • Brünger, A.T.1
  • 45
    • 0000243829 scopus 로고
    • PROCHECK - A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., Macauthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK - A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacAuthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 46
    • 0014381393 scopus 로고
    • Conformations of polypeptides and proteins
    • Ramachandran, S. (1968). Conformations of polypeptides and proteins. Adv. Prot. Chem. 23, 283-437.
    • (1968) Adv. Prot. Chem. , vol.23 , pp. 283-437
    • Ramachandran, S.1
  • 47
    • 0000082544 scopus 로고
    • Chain - A crystallographic modeling program
    • Sack, J.S. (1988). Chain - A crystallographic modeling program. J. Mol. Graphics 6, 224-225.
    • (1988) J. Mol. Graphics , vol.6 , pp. 224-225
    • Sack, J.S.1
  • 48
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (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
  • 50
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993). ALSCRIPT: A tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.