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Volumn 110, Issue 21, 2013, Pages 8519-8524

X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification

Author keywords

Iron sulfur cluster fold; Radical SAM dehydrogenase

Indexed keywords

CYSTEINE; GLYCINE DERIVATIVE; OXIDOREDUCTASE; S ADENOSYLMETHIONINE; SERINE; SULFATASE;

EID: 84878137190     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1302417110     Document Type: Article
Times cited : (103)

References (40)
  • 1
    • 0029130352 scopus 로고
    • A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
    • Schmidt B, Selmer T, Ingendoh A, von Figura K (1995) A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell 82(2): 271-278.
    • (1995) Cell , vol.82 , Issue.2 , pp. 271-278
    • Schmidt, B.1    Selmer, T.2    Ingendoh, A.3    Von Figura, K.4
  • 2
    • 34447618279 scopus 로고    scopus 로고
    • Human sulfatases: A structural perspective to catalysis
    • Ghosh D (2007) Human sulfatases: A structural perspective to catalysis. Cell Mol Life Sci 64(15): 2013-2022.
    • (2007) Cell Mol Life Sci , vol.64 , Issue.15 , pp. 2013-2022
    • Ghosh, D.1
  • 3
    • 53849125403 scopus 로고    scopus 로고
    • Sulfotransferases, sulfatases and formylglycine-generating enzymes: A sulfation fascination
    • Bojarová P, Williams SJ (2008) Sulfotransferases, sulfatases and formylglycine-generating enzymes: A sulfation fascination. Curr Opin Chem Biol 12(5): 573-581.
    • (2008) Curr Opin Chem Biol , vol.12 , Issue.5 , pp. 573-581
    • Bojarová, P.1    Williams, S.J.2
  • 4
    • 0037847425 scopus 로고    scopus 로고
    • Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme
    • Dierks T, et al. (2003) Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme. Cell 113(4): 435-444.
    • (2003) Cell , vol.113 , Issue.4 , pp. 435-444
    • Dierks, T.1
  • 5
    • 79960418118 scopus 로고    scopus 로고
    • Sulfatases and a radical AdoMet enzyme are key for mucosal glycan foraging and fitness of a prominent human gut Bacteroides
    • Benjdia A, Martens EC, Gordon JI, Berteau O (2011) Sulfatases and a radical AdoMet enzyme are key for mucosal glycan foraging and fitness of a prominent human gut Bacteroides. J Biol Chem 286(29): 25973-25982.
    • (2011) J Biol Chem , vol.286 , Issue.29 , pp. 25973-25982
    • Benjdia, A.1    Martens, E.C.2    Gordon, J.I.3    Berteau, O.4
  • 6
    • 19344367884 scopus 로고    scopus 로고
    • Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme
    • Dierks T, et al. (2005) Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine- generating enzyme. Cell 121(4): 541-552.
    • (2005) Cell , vol.121 , Issue.4 , pp. 541-552
    • Dierks, T.1
  • 7
    • 30444449938 scopus 로고    scopus 로고
    • A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme
    • Roeser D, et al. (2006) A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. Proc Natl Acad Sci USA 103(1): 81-86.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.1 , pp. 81-86
    • Roeser, D.1
  • 8
    • 2442499333 scopus 로고    scopus 로고
    • Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB
    • Fang Q, Peng J, Dierks T (2004) Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB. J Biol Chem 279(15): 14570-14578.
    • (2004) J Biol Chem , vol.279 , Issue.15 , pp. 14570-14578
    • Fang, Q.1    Peng, J.2    Dierks, T.3
  • 9
    • 33947655766 scopus 로고    scopus 로고
    • Anaerobic sulfatase-maturating enzymes: Radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification
    • Benjdia A, et al. (2007) Anaerobic sulfatase-maturating enzymes: Radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification. J Am Chem Soc 129(12): 3462-3463.
    • (2007) J Am Chem Soc , vol.129 , Issue.12 , pp. 3462-3463
    • Benjdia, A.1
  • 10
    • 47349101467 scopus 로고    scopus 로고
    • In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters
    • Grove TL, Lee KH, St Clair J, Krebs C, Booker SJ (2008) In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters. Biochemistry 47(28): 7523-7538.
    • (2008) Biochemistry , vol.47 , Issue.28 , pp. 7523-7538
    • Grove, T.L.1    Lee, K.H.2    St Clair, J.3    Krebs, C.4    Booker, S.J.5
  • 11
    • 33747330135 scopus 로고    scopus 로고
    • A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes
    • Berteau O, Guillot A, Benjdia A, Rabot S (2006) A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes. J Biol Chem 281(32): 22464-22470.
    • (2006) J Biol Chem , vol.281 , Issue.32 , pp. 22464-22470
    • Berteau, O.1    Guillot, A.2    Benjdia, A.3    Rabot, S.4
  • 12
    • 84861034877 scopus 로고    scopus 로고
    • Site-specific chemical protein conjugation using genetically encoded aldehyde tags
    • Rabuka D, Rush JS, deHart GW, Wu P, Bertozzi CR (2012) Site-specific chemical protein conjugation using genetically encoded aldehyde tags. Nat Protoc 7(6): 1052-1067.
    • (2012) Nat Protoc , vol.7 , Issue.6 , pp. 1052-1067
    • Rabuka, D.1    Rush, J.S.2    Dehart, G.W.3    Wu, P.4    Bertozzi, C.R.5
  • 14
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE (2001) Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods. Nucleic Acids Res 29(5): 1097-1106.
    • (2001) Nucleic Acids Res , vol.29 , Issue.5 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 15
    • 84866046539 scopus 로고    scopus 로고
    • Enzyme catalyzed formation of radicals from S-adenosylmethionine and inhibition of enzyme activity by the cleavage products
    • Hiscox MJ, Driesener RC, Roach PL (2012) Enzyme catalyzed formation of radicals from S-adenosylmethionine and inhibition of enzyme activity by the cleavage products. Biochim Biophys Acta 1824(11): 1165-1177.
    • (2012) Biochim Biophys Acta , vol.1824 , Issue.11 , pp. 1165-1177
    • Hiscox, M.J.1    Driesener, R.C.2    Roach, P.L.3
  • 16
    • 0037174377 scopus 로고    scopus 로고
    • An anchoring role for FeS clusters: Chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme
    • Walsby CJ, Ortillo D, Broderick WE, Broderick JB, Hoffman BM (2002) An anchoring role for FeS clusters: Chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme. J Am Chem Soc 124(38): 11270-11271.
    • (2002) J Am Chem Soc , vol.124 , Issue.38 , pp. 11270-11271
    • Walsby, C.J.1    Ortillo, D.2    Broderick, W.E.3    Broderick, J.B.4    Hoffman, B.M.5
  • 17
    • 77950463535 scopus 로고    scopus 로고
    • Anaerobic sulfatase-maturating enzyme - A mechanistic link with glycyl radical-activating enzymes?
    • Benjdia A, et al. (2010) Anaerobic sulfatase-maturating enzyme - A mechanistic link with glycyl radical-activating enzymes? FEBS J 277(8): 1906-1920.
    • (2010) FEBS J , vol.277 , Issue.8 , pp. 1906-1920
    • Benjdia, A.1
  • 18
    • 50149113479 scopus 로고    scopus 로고
    • Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy
    • Yokoyama K, Ohmori D, Kudo F, Eguchi T (2008) Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy. Biochemistry 47(34): 8950-8960.
    • (2008) Biochemistry , vol.47 , Issue.34 , pp. 8950-8960
    • Yokoyama, K.1    Ohmori, D.2    Kudo, F.3    Eguchi, T.4
  • 19
    • 37049024768 scopus 로고    scopus 로고
    • Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin
    • Yokoyama K, Numakura M, Kudo F, Ohmori D, Eguchi T (2007) Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin. J Am Chem Soc 129(49): 15147-15155.
    • (2007) J Am Chem Soc , vol.129 , Issue.49 , pp. 15147-15155
    • Yokoyama, K.1    Numakura, M.2    Kudo, F.3    Ohmori, D.4    Eguchi, T.5
  • 20
    • 84866011930 scopus 로고    scopus 로고
    • Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes
    • Lanz ND, Booker SJ (2012) Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes. Biochim Biophys Acta 1824(11): 1196-1212.
    • (2012) Biochim Biophys Acta , vol.1824 , Issue.11 , pp. 1196-1212
    • Lanz, N.D.1    Booker, S.J.2
  • 21
    • 77951930923 scopus 로고    scopus 로고
    • A consensus mechanism for radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters
    • Grove TL, Ahlum JH, Sharma P, Krebs C, Booker SJ (2010) A consensus mechanism for radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters. Biochemistry 49(18): 3783-3785.
    • (2010) Biochemistry , vol.49 , Issue.18 , pp. 3783-3785
    • Grove, T.L.1    Ahlum, J.H.2    Sharma, P.3    Krebs, C.4    Booker, S.J.5
  • 22
    • 79958173211 scopus 로고    scopus 로고
    • Biological systems discovery in silico: Radical S-adenosylmethionine protein families and their target peptides for posttranslational modification
    • Haft DH, Basu MK (2011) Biological systems discovery in silico: Radical S-adenosylmethionine protein families and their target peptides for posttranslational modification. J Bacteriol 193(11): 2745-2755.
    • (2011) J Bacteriol , vol.193 , Issue.11 , pp. 2745-2755
    • Haft, D.H.1    Basu, M.K.2
  • 23
    • 78651081719 scopus 로고    scopus 로고
    • Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners
    • Haft DH (2011) Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners. BMC Genomics 12:21.
    • (2011) BMC Genomics , vol.12 , pp. 21
    • Haft, D.H.1
  • 24
    • 67649976798 scopus 로고    scopus 로고
    • ENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II of the S-adenosylmethionine-dependent enzyme MoaA: Mechanistic implications
    • Lees NS, et al. (2009) ENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II of the S-adenosylmethionine-dependent enzyme MoaA: Mechanistic implications. J Am Chem Soc 131(26): 9184-9185.
    • (2009) J Am Chem Soc , vol.131 , Issue.26 , pp. 9184-9185
    • Lees, N.S.1
  • 25
    • 33646468635 scopus 로고    scopus 로고
    • Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism
    • Hänzelmann P, Schindelin H (2006) Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism. Proc Natl Acad Sci USA 103(18): 6829-6834.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.18 , pp. 6829-6834
    • Hänzelmann, P.1    Schindelin, H.2
  • 26
    • 84877062815 scopus 로고    scopus 로고
    • Further characterization of Cys-type and Ser-type anaerobic sulfatase maturating enzymes suggests a commonality in mechanism of catalysis
    • 10.1021/bi400136u
    • Grove TL, et al. (2013) Further characterization of Cys-type and Ser-type anaerobic sulfatase maturating enzymes suggests a commonality in mechanism of catalysis. Biochemistry, 10.1021/bi400136u.
    • (2013) Biochemistry
    • Grove, T.L.1
  • 27
    • 49649128470 scopus 로고    scopus 로고
    • Anaerobic sulfatase-maturating enzymes, first dual substrate radical S-adenosylmethionine enzymes
    • Benjdia A, et al. (2008) Anaerobic sulfatase-maturating enzymes, first dual substrate radical S-adenosylmethionine enzymes. J Biol Chem 283(26): 17815-17826.
    • (2008) J Biol Chem , vol.283 , Issue.26 , pp. 17815-17826
    • Benjdia, A.1
  • 28
    • 79954499453 scopus 로고    scopus 로고
    • Structural insights into radical generation by the radical SAM superfamily
    • Vey JL, Drennan CL (2011) Structural insights into radical generation by the radical SAM superfamily. Chem Rev 111(4): 2487-2506.
    • (2011) Chem Rev , vol.111 , Issue.4 , pp. 2487-2506
    • Vey, J.L.1    Drennan, C.L.2
  • 29
    • 84866021687 scopus 로고    scopus 로고
    • Structural diversity in the AdoMet radical enzyme superfamily
    • Dowling DP, Vey JL, Croft AK, Drennan CL (2012) Structural diversity in the AdoMet radical enzyme superfamily. Biochim Biophys Acta 1824(11): 1178-1195.
    • (2012) Biochim Biophys Acta , vol.1824 , Issue.11 , pp. 1178-1195
    • Dowling, D.P.1    Vey, J.L.2    Croft, A.K.3    Drennan, C.L.4
  • 30
    • 0347504850 scopus 로고    scopus 로고
    • Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes
    • Layer G, Moser J, Heinz DW, Jahn D, Schubert WD (2003) Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes. EMBO J 22(23): 6214-6224.
    • (2003) EMBO J , vol.22 , Issue.23 , pp. 6214-6224
    • Layer, G.1    Moser, J.2    Heinz, D.W.3    Jahn, D.4    Schubert, W.D.5
  • 31
    • 70349381588 scopus 로고    scopus 로고
    • Unexpected electron transfer mechanism upon AdoMet cleavage in radical SAM proteins
    • Nicolet Y, Amara P, Mouesca JM, Fontecilla-Camps JC (2009) Unexpected electron transfer mechanism upon AdoMet cleavage in radical SAM proteins. Proc Natl Acad Sci USA 106(35): 14867-14871.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.35 , pp. 14867-14871
    • Nicolet, Y.1    Amara, P.2    Mouesca, J.M.3    Fontecilla-Camps, J.C.4
  • 32
    • 55849139092 scopus 로고    scopus 로고
    • Structural basis for glycyl radical formation by pyruvate formatelyase activating enzyme
    • Vey JL, et al. (2008) Structural basis for glycyl radical formation by pyruvate formatelyase activating enzyme. Proc Natl Acad Sci USA 105(42): 16137-16141.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.42 , pp. 16137-16141
    • Vey, J.L.1
  • 33
    • 4444346402 scopus 로고    scopus 로고
    • Crystal structure of the S-adenosylmethioninedependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans
    • Hänzelmann P, Schindelin H (2004) Crystal structure of the S-adenosylmethioninedependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans. Proc Natl Acad Sci USA 101(35): 12870-12875.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.35 , pp. 12870-12875
    • Hänzelmann, P.1    Schindelin, H.2
  • 34
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372(3): 774-797.
    • (2007) J Mol Biol , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 36
    • 79955526574 scopus 로고    scopus 로고
    • A radically different mechanism for S-adenosylmethioninedependent methyltransferases
    • Grove TL, et al. (2011) A radically different mechanism for S-adenosylmethioninedependent methyltransferases. Science 332(6029): 604-607.
    • (2011) Science , vol.332 , Issue.6029 , pp. 604-607
    • Grove, T.L.1
  • 37
    • 70350113877 scopus 로고    scopus 로고
    • Characterization and mechanistic studies of DesII: A radical S-adenosyl-L-methionine enzyme involved in the biosynthesis of TDP-D-desosamine
    • Szu PH, Ruszczycky MW, Choi SH, Yan F, Liu HW (2009) Characterization and mechanistic studies of DesII: A radical S-adenosyl-L-methionine enzyme involved in the biosynthesis of TDP-D-desosamine. J Am Chem Soc 131(39): 14030-14042.
    • (2009) J Am Chem Soc , vol.131 , Issue.39 , pp. 14030-14042
    • Szu, P.H.1    Ruszczycky, M.W.2    Choi, S.H.3    Yan, F.4    Liu, H.W.5
  • 38
    • 81255138862 scopus 로고    scopus 로고
    • The enzyme function initiative
    • Gerlt JA, et al. (2011) The Enzyme Function Initiative. Biochemistry 50(46): 9950-9962.
    • (2011) Biochemistry , vol.50 , Issue.46 , pp. 9950-9962
    • Gerlt, J.A.1
  • 39
    • 84874066127 scopus 로고    scopus 로고
    • Catalysis of a new ribose carbon-insertion reaction by the molybdenum cofactor biosynthetic enzyme MoaA
    • Mehta AP, et al. (2013) Catalysis of a new ribose carbon-insertion reaction by the molybdenum cofactor biosynthetic enzyme MoaA. Biochemistry 52(7): 1134-1136.
    • (2013) Biochemistry , vol.52 , Issue.7 , pp. 1134-1136
    • Mehta, A.P.1
  • 40
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy H, Erez E, Martz E, Pupko T, Ben-Tal N (2010) ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res 38(Web Server issue):W529-W533.
    • (2010) Nucleic Acids Res , vol.38 , Issue.WEB SERVER ISSUE
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5


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