메뉴 건너뛰기




Volumn 385, Issue 5, 2009, Pages 1456-1469

Structure of Selenophosphate Synthetase Essential for Selenium Incorporation into Proteins and RNAs

Author keywords

PurM superfamily; SelD; selenocysteine; selenoprotein; X ray crystallography

Indexed keywords

ADENOSINE DIPHOSPHATE; HOMODIMER; METAL ION; NUCLEOPHILE; SELENIUM; SELENOPHOSPHATE SYNTHETASE; SELENOPROTEIN; UNCLASSIFIED DRUG;

EID: 58549089314     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.08.042     Document Type: Article
Times cited : (35)

References (40)
  • 2
    • 0027144016 scopus 로고
    • Monoselenophosphate: synthesis, characterization, and identity with the prokaryotic biological selenium donor, compound SePX
    • Glass R.S., Singh W.P., Jung W., Veres Z., Scholz T.D., and Stadtman T.C. Monoselenophosphate: synthesis, characterization, and identity with the prokaryotic biological selenium donor, compound SePX. Biochemistry 32 (1993) 12555-12559
    • (1993) Biochemistry , vol.32 , pp. 12555-12559
    • Glass, R.S.1    Singh, W.P.2    Jung, W.3    Veres, Z.4    Scholz, T.D.5    Stadtman, T.C.6
  • 3
    • 0026625738 scopus 로고
    • Selenoprotein synthesis in E. coli. Purification and characterisation of the enzyme catalysing selenium activation
    • Ehrenreich A., Forchhammer K., Tormay P., Veprek B., and Böck A. Selenoprotein synthesis in E. coli. Purification and characterisation of the enzyme catalysing selenium activation. Eur. J. Biochem. 206 (1992) 767-773
    • (1992) Eur. J. Biochem. , vol.206 , pp. 767-773
    • Ehrenreich, A.1    Forchhammer, K.2    Tormay, P.3    Veprek, B.4    Böck, A.5
  • 4
    • 0028289519 scopus 로고
    • Selenophosphate synthetase. Enzyme properties and catalytic reaction
    • Veres Z., Kim I.Y., Scholz T.D., and Stadtman T.C. Selenophosphate synthetase. Enzyme properties and catalytic reaction. J. Biol. Chem. 269 (1994) 10597-10603
    • (1994) J. Biol. Chem. , vol.269 , pp. 10597-10603
    • Veres, Z.1    Kim, I.Y.2    Scholz, T.D.3    Stadtman, T.C.4
  • 5
    • 4043055054 scopus 로고    scopus 로고
    • Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography
    • Anand R., Hoskins A.A., Stubbe J., and Ealick S.E. Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography. Biochemistry 43 (2004) 10328-10342
    • (2004) Biochemistry , vol.43 , pp. 10328-10342
    • Anand, R.1    Hoskins, A.A.2    Stubbe, J.3    Ealick, S.E.4
  • 6
    • 33845582675 scopus 로고    scopus 로고
    • Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily
    • Morar M., Anand R., Hoskins A.A., Stubbe J., and Ealick S.E. Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily. Biochemistry 45 (2006) 14880-14895
    • (2006) Biochemistry , vol.45 , pp. 14880-14895
    • Morar, M.1    Anand, R.2    Hoskins, A.A.3    Stubbe, J.4    Ealick, S.E.5
  • 7
    • 18244430454 scopus 로고    scopus 로고
    • SelD homolog from Drosophila lacking selenide-dependent monoselenophosphate synthetase activity
    • Persson B.C., Böck A., Jackle H., and Vorbruggen G. SelD homolog from Drosophila lacking selenide-dependent monoselenophosphate synthetase activity. J. Mol. Biol. 274 (1997) 174-180
    • (1997) J. Mol. Biol. , vol.274 , pp. 174-180
    • Persson, B.C.1    Böck, A.2    Jackle, H.3    Vorbruggen, G.4
  • 9
    • 0023907071 scopus 로고
    • Gene for a novel tRNA species that accepts l-serine and cotranslationally inserts selenocysteine
    • Leinfelder W., Zehelein E., Mandrand-Berthelot M.A., and Böck A. Gene for a novel tRNA species that accepts l-serine and cotranslationally inserts selenocysteine. Nature 331 (1988) 723-725
    • (1988) Nature , vol.331 , pp. 723-725
    • Leinfelder, W.1    Zehelein, E.2    Mandrand-Berthelot, M.A.3    Böck, A.4
  • 10
    • 33845763611 scopus 로고    scopus 로고
    • RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea
    • Yuan J., Palioura S., Salazar J.C., Su D., O'Donoghue P., Hohn M.J., et al. RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea. Proc. Natl Acad. Sci. USA 103 (2006) 18923-18927
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 18923-18927
    • Yuan, J.1    Palioura, S.2    Salazar, J.C.3    Su, D.4    O'Donoghue, P.5    Hohn, M.J.6
  • 11
    • 0033632277 scopus 로고    scopus 로고
    • Biosynthesis of selenoproteins-an overview
    • Böck A. Biosynthesis of selenoproteins-an overview. Biofactors 11 (2000) 77-78
    • (2000) Biofactors , vol.11 , pp. 77-78
    • Böck, A.1
  • 12
    • 0022502192 scopus 로고
    • Biosynthesis of 5-methylaminomethyl-2-selenouridine, a naturally occurring nucleoside in Escherichia coli tRNA
    • Wittwer A.J., and Stadtman T.C. Biosynthesis of 5-methylaminomethyl-2-selenouridine, a naturally occurring nucleoside in Escherichia coli tRNA. Arch. Biochem. Biophys. 248 (1986) 540-550
    • (1986) Arch. Biochem. Biophys. , vol.248 , pp. 540-550
    • Wittwer, A.J.1    Stadtman, T.C.2
  • 13
    • 0028144791 scopus 로고
    • A purified selenophosphate-dependent enzyme from Salmonella typhimurium catalyzes the replacement of sulfur in 2-thiouridine residues in tRNAs with selenium
    • Veres Z., and Stadtman T.C. A purified selenophosphate-dependent enzyme from Salmonella typhimurium catalyzes the replacement of sulfur in 2-thiouridine residues in tRNAs with selenium. Proc. Natl Acad. Sci. USA 91 (1994) 8092-8096
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8092-8096
    • Veres, Z.1    Stadtman, T.C.2
  • 14
    • 0030847993 scopus 로고    scopus 로고
    • Identification of a phosphorylated enzyme intermediate in the catalytic mechanism for selenophosphate synthetase
    • Mullins L.S., Hong S.-B., Gibson G.E., Walker H., Stadtman T.C., and Raushel F.M. Identification of a phosphorylated enzyme intermediate in the catalytic mechanism for selenophosphate synthetase. J. Am. Chem. Soc. 119 (1997) 6684-6685
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6684-6685
    • Mullins, L.S.1    Hong, S.-B.2    Gibson, G.E.3    Walker, H.4    Stadtman, T.C.5    Raushel, F.M.6
  • 15
    • 0032478141 scopus 로고    scopus 로고
    • Isotope exchange studies on the Escherichia coli selenophosphate synthetase mechanism
    • Walker H., Ferretti J.A., and Stadtman T.C. Isotope exchange studies on the Escherichia coli selenophosphate synthetase mechanism. Proc. Natl Acad. Sci. USA 95 (1998) 2180-2185
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 2180-2185
    • Walker, H.1    Ferretti, J.A.2    Stadtman, T.C.3
  • 16
    • 0026779417 scopus 로고
    • Escherichia coli mutant SELD enzymes. The cysteine 17 residue is essential for selenophosphate formation from ATP and selenide
    • Kim I.Y., Veres Z., and Stadtman T.C. Escherichia coli mutant SELD enzymes. The cysteine 17 residue is essential for selenophosphate formation from ATP and selenide. J. Biol. Chem. 267 (1992) 19650-19654
    • (1992) J. Biol. Chem. , vol.267 , pp. 19650-19654
    • Kim, I.Y.1    Veres, Z.2    Stadtman, T.C.3
  • 17
    • 0001172445 scopus 로고
    • Biochemical analysis of Escherichia coli selenophosphate synthetase mutants. Lysine 20 is essential for catalytic activity and cysteine 17/19 for 8-azido-ATP derivatization
    • Kim I.Y., Veres Z., and Stadtman T.C. Biochemical analysis of Escherichia coli selenophosphate synthetase mutants. Lysine 20 is essential for catalytic activity and cysteine 17/19 for 8-azido-ATP derivatization. J. Biol. Chem. 268 (1993) 27020-27025
    • (1993) J. Biol. Chem. , vol.268 , pp. 27020-27025
    • Kim, I.Y.1    Veres, Z.2    Stadtman, T.C.3
  • 19
    • 0033524427 scopus 로고    scopus 로고
    • Catalytic properties of selenophosphate synthetases: comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli
    • Lacourciere G.M., and Stadtman T.C. Catalytic properties of selenophosphate synthetases: comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli. Proc. Natl Acad. Sci. USA 96 (1999) 44-48
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 44-48
    • Lacourciere, G.M.1    Stadtman, T.C.2
  • 20
    • 0000301355 scopus 로고    scopus 로고
    • Fetal mouse selenophosphate synthetase 2 (SPS2): characterization of the cysteine mutant form overproduced in a baculovirus-insect cell system
    • Kim I.Y., Guimaraes M.J., Zlotnik A., Bazan J.F., and Stadtman T.C. Fetal mouse selenophosphate synthetase 2 (SPS2): characterization of the cysteine mutant form overproduced in a baculovirus-insect cell system. Proc. Natl Acad. Sci. USA 94 (1997) 418-421
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 418-421
    • Kim, I.Y.1    Guimaraes, M.J.2    Zlotnik, A.3    Bazan, J.F.4    Stadtman, T.C.5
  • 21
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • Zheng L., White R.H., Cash V.L., Jack R.F., and Dean D.R. Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc. Natl Acad. Sci. USA 90 (1993) 2754-2758
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 22
    • 0032553428 scopus 로고    scopus 로고
    • The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphate
    • Lacourciere G.M., and Stadtman T.C. The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphate. J. Biol. Chem. 273 (1998) 30921-30926
    • (1998) J. Biol. Chem. , vol.273 , pp. 30921-30926
    • Lacourciere, G.M.1    Stadtman, T.C.2
  • 23
    • 0034604544 scopus 로고    scopus 로고
    • Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate
    • Lacourciere G.M., Mihara H., Kurihara T., Esaki N., and Stadtman T.C. Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate. J. Biol. Chem. 275 (2000) 23769-23773
    • (2000) J. Biol. Chem. , vol.275 , pp. 23769-23773
    • Lacourciere, G.M.1    Mihara, H.2    Kurihara, T.3    Esaki, N.4    Stadtman, T.C.5
  • 24
    • 46249126434 scopus 로고    scopus 로고
    • Crystal structure of an N-terminally-truncated selenophosphate synthetase from Aquifex aeolicus
    • Matsumoto E., Sekine S., Akasaka R., Otta Y., Katsura K., Inoue M., et al. Crystal structure of an N-terminally-truncated selenophosphate synthetase from Aquifex aeolicus. Acta Crystallogr Sect. F 64 (2008) 453-458
    • (2008) Acta Crystallogr Sect. F , vol.64 , pp. 453-458
    • Matsumoto, E.1    Sekine, S.2    Akasaka, R.3    Otta, Y.4    Katsura, K.5    Inoue, M.6
  • 25
    • 0001007592 scopus 로고    scopus 로고
    • X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2. 5 Å resolution
    • Li C., Kappock T.J., Stubbe J., Weaver T.M., and Ealick S.E. X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2. 5 Å resolution. Structure 7 (1999) 1155-1166
    • (1999) Structure , vol.7 , pp. 1155-1166
    • Li, C.1    Kappock, T.J.2    Stubbe, J.3    Weaver, T.M.4    Ealick, S.E.5
  • 26
    • 34250874525 scopus 로고    scopus 로고
    • Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: insights into cyanation reaction by thiol redox signaling
    • Watanabe S., Matsumi R., Arai T., Atomi H., Imanaka T., and Miki K. Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: insights into cyanation reaction by thiol redox signaling. Mol. Cell 27 (2007) 29-40
    • (2007) Mol. Cell , vol.27 , pp. 29-40
    • Watanabe, S.1    Matsumi, R.2    Arai, T.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 27
    • 41149144136 scopus 로고    scopus 로고
    • Structural studies of thiamin monophosphate kinase in complex with substrates and products
    • McCulloch K.M., Kinsland C., Begley T.P., and Ealick S.E. Structural studies of thiamin monophosphate kinase in complex with substrates and products. Biochemistry 47 (2008) 3810-3821
    • (2008) Biochemistry , vol.47 , pp. 3810-3821
    • McCulloch, K.M.1    Kinsland, C.2    Begley, T.P.3    Ealick, S.E.4
  • 29
    • 0021152409 scopus 로고
    • The nutritional biochemistry of selenium
    • Combs G.F.J., and Combs S.B. The nutritional biochemistry of selenium. Annu. Rev. Nutr. 4 (1984) 257-280
    • (1984) Annu. Rev. Nutr. , vol.4 , pp. 257-280
    • Combs, G.F.J.1    Combs, S.B.2
  • 32
    • 0034636007 scopus 로고    scopus 로고
    • Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis
    • Clausen T., Kaiser J.T., Steegborn C., Huber R., and Kessler D. Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis. Proc. Natl Acad. Sci. USA 97 (2000) 3856-3861
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3856-3861
    • Clausen, T.1    Kaiser, J.T.2    Steegborn, C.3    Huber, R.4    Kessler, D.5
  • 36
    • 0036303444 scopus 로고    scopus 로고
    • Analysis of the E. coli NifS CsdB protein at 2. 0 Å reveals the structural basis for perselenide and persulfide intermediate formation
    • Lima C.D. Analysis of the E. coli NifS CsdB protein at 2. 0 Å reveals the structural basis for perselenide and persulfide intermediate formation. J. Mol. Biol. 315 (2002) 1199-1208
    • (2002) J. Mol. Biol. , vol.315 , pp. 1199-1208
    • Lima, C.D.1
  • 37
    • 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
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-325
    • (1997) Methods Enzymol. , vol.276 , pp. 307-325
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 40
    • 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 M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. Sect. A. 47 (1991) 110-119
    • (1991) Acta Crystallogr. Sect. A. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.