메뉴 건너뛰기




Volumn 32, Issue 13, 2004, Pages 4015-4025

AdoMet radical proteins - From structure to evolution - Alignment of divergent protein sequences reveals strong secondary structure element conservation

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN SYNTHASE; COPROPORPHYRINOGEN OXIDASE; DNA; RIBONUCLEOTIDE REDUCTASE; RIBONUCLEOTIDE REDUCTASE ACTIVASE; RNA; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG; FLAVODOXIN; FREE RADICAL;

EID: 3242882336     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh728     Document Type: Article
Times cited : (94)

References (36)
  • 1
    • 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,H.J., Chen,G., Hetzler,B.G., Reyes-Spindola,J.F. and Miller,N.E. (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, 1097-1106.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 2
    • 0034792676 scopus 로고    scopus 로고
    • Radical mechanisms of S-adenosylmethionine-dependent enzymes
    • Frey,P.A. and Booker,S.J. (2001) Radical mechanisms of S-adenosylmethionine-dependent enzymes. Adv. Protein Chem., 58, 1-45.
    • (2001) Adv. Protein Chem. , vol.58 , pp. 1-45
    • Frey, P.A.1    Booker, S.J.2
  • 3
    • 0033969775 scopus 로고    scopus 로고
    • Mutagenesis of the proposed iron-sulfur cluster binding ligands in Escherichia coli biotin synthase
    • Hewitson,K.S., Baldwin,J.E., Shaw,N.M. and Roach,P.L. (2000) Mutagenesis of the proposed iron-sulfur cluster binding ligands in Escherichia coli biotin synthase. FEBS Lett., 466, 372-376.
    • (2000) FEBS Lett. , vol.466 , pp. 372-376
    • Hewitson, K.S.1    Baldwin, J.E.2    Shaw, N.M.3    Roach, P.L.4
  • 5
    • 0037072870 scopus 로고    scopus 로고
    • Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
    • Layer,G., Verfurth,K., Mahlitz,E. and Jahn,D. (2002) Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli. J. Biol. Chem., 277, 34136-34142.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34136-34142
    • Layer, G.1    Verfurth, K.2    Mahlitz, E.3    Jahn, D.4
  • 6
    • 0034717328 scopus 로고    scopus 로고
    • The activating component of the anaerobic ribonucleotide reductase from Escherichia coli. An iron-sulfur center with only three cysteines
    • Tamarit,J., Gerez,C., Meier,C., Mulliez,E., Trautwein,A. and Fontecave,M. (2000) The activating component of the anaerobic ribonucleotide reductase from Escherichia coli. An iron-sulfur center with only three cysteines. J. Biol. Chem., 275, 15669-15675.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15669-15675
    • Tamarit, J.1    Gerez, C.2    Meier, C.3    Mulliez, E.4    Trautwein, A.5    Fontecave, M.6
  • 8
    • 0034841061 scopus 로고    scopus 로고
    • Adenosylmethionine-dependent iron-sulfur enzymes: Versatile clusters in a radical new role
    • Cheek,J. and Broderick,J.B. (2001) Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new role. J. Biol. Inorg. Chem., 6, 209-226.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 209-226
    • Cheek, J.1    Broderick, J.B.2
  • 9
    • 0037399004 scopus 로고    scopus 로고
    • The generation of 5′-deoxyadenosyl radicals by adenosylmethionine-dependent radical enzymes
    • Jarrett,J.T. (2003) The generation of 5′-deoxyadenosyl radicals by adenosylmethionine-dependent radical enzymes. Curr. Opin. Chem. Biol., 7, 174-182.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 174-182
    • Jarrett, J.T.1
  • 10
    • 0346727529 scopus 로고    scopus 로고
    • Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
    • Berkovitch,F., Nicolet,Y., Wan,J.T., Jarrett,J.T. and Drennan,C.L. (2004) Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science, 303, 76-79.
    • (2004) Science , vol.303 , pp. 76-79
    • Berkovitch, F.1    Nicolet, Y.2    Wan, J.T.3    Jarrett, J.T.4    Drennan, C.L.5
  • 11
    • 0347504850 scopus 로고    scopus 로고
    • Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes
    • Layer,G., Moser,J., Heinz,D.W., Jahn,D. and Schubert,W.D. (2003) Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes. EMBO J., 22, 6214-6224.
    • (2003) EMBO J. , vol.22 , pp. 6214-6224
    • Layer, G.1    Moser, J.2    Heinz, D.W.3    Jahn, D.4    Schubert, W.D.5
  • 12
    • 0037396345 scopus 로고    scopus 로고
    • Evolution of function in (beta/ alpha)8-barrel enzymes
    • Gerlt,J.A. and Raushel,F.M. (2003) Evolution of function in (beta/ alpha)8-barrel enzymes. Curr. Opin. Chem. Biol., 7, 252-264.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 252-264
    • Gerlt, J.A.1    Raushel, F.M.2
  • 13
    • 0347625651 scopus 로고    scopus 로고
    • Identification of the 7,8-didemethyl-8-hydroxyz-5-deazariboflavin synthase required for coenzyme F420 biosythesis
    • Graham,D.E., Xu,H.M. and White,R.H. (2003) Identification of the 7,8-didemethyl-8-hydroxyz-5-deazariboflavin synthase required for coenzyme F420 biosythesis. Arch. Microbiol., 180, 455-464.
    • (2003) Arch. Microbiol. , vol.180 , pp. 455-464
    • Graham, D.E.1    Xu, H.M.2    White, R.H.3
  • 16
    • 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. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 17
    • 0003932768 scopus 로고
    • 1st edn. W.H. Freeman and Company, New York, NY
    • Creighton,T.E. (1984) Proteins, 1st edn. W.H. Freeman and Company, New York, NY.
    • (1984) Proteins
    • Creighton, T.E.1
  • 19
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch,W. and Sander,C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 20
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet,P., Courcelle,E., Stuart,D.I. and Metoz,F. (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics, 15, 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 21
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information
    • Gouet,P., Robert,X. and Courcelle,E. (2003) ESPript/ENDscript: extracting and rendering sequence and 3D information. Nucleic Acids Res., 31, 3320-3323.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 22
    • 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,C.J., Ortillo,D., Broderick,W.E., Broderick,J.B. and Hoffman,B.M. (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, 11270-11271.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11270-11271
    • Walsby, C.J.1    Ortillo, D.2    Broderick, W.E.3    Broderick, J.B.4    Hoffman, B.M.5
  • 23
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: A chronicle of convergence
    • Schubert,H.L., Blumenthal,R.M. and Cheng,X. (2003) Many paths to methyltransfer: a chronicle of convergence. Trends Biochem. Sci., 28, 329-335.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 24
    • 0030610719 scopus 로고    scopus 로고
    • AlF3 mimics the transition state of protein phosphorylation in the crystal structure of nucleoside diphosphate kinase and MgADP
    • Xu,Y.W., Morera,S., Janin,J. and Cherfils,J. (1997) AlF3 mimics the transition state of protein phosphorylation in the crystal structure of nucleoside diphosphate kinase and MgADP. Proc. Natl Acad. Sci. USA, 94, 3579-3583.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3579-3583
    • Xu, Y.W.1    Morera, S.2    Janin, J.3    Cherfils, J.4
  • 25
    • 0037082119 scopus 로고    scopus 로고
    • Ribonucleotide reductases: The evolution of allosteric regulation
    • Reichard,P. (2002) Ribonucleotide reductases: the evolution of allosteric regulation. Arch. Biochem. Biophys., 397, 149-155.
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 149-155
    • Reichard, P.1
  • 27
    • 0031980567 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of benzylsuccinate synthase from Thauera aromatica: A new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism
    • Leuthner,B., Leutwein,C., Schulz,H., Horth,P., Haehnel,W., Schiltz,E., Schagger,H. and Heider,J. (1998) Biochemical and genetic characterization of benzylsuccinate synthase from Thauera aromatica: a new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism. Mol. Microbiol., 28, 615-628.
    • (1998) Mol. Microbiol. , vol.28 , pp. 615-628
    • Leuthner, B.1    Leutwein, C.2    Schulz, H.3    Horth, P.4    Haehnel, W.5    Schiltz, E.6    Schagger, H.7    Heider, J.8
  • 28
  • 30
    • 0033525599 scopus 로고    scopus 로고
    • A glycyl radical site in the crystal structure of a class III ribonucleotide reductase
    • Logan,D.T., Andersson,J., Sjöberg,B.-M. and Nordlund,P. (1999) A glycyl radical site in the crystal structure of a class III ribonucleotide reductase. Science, 283, 1499-1504.
    • (1999) Science , vol.283 , pp. 1499-1504
    • Logan, D.T.1    Andersson, J.2    Sjöberg, B.-M.3    Nordlund, P.4
  • 31
    • 0034284955 scopus 로고    scopus 로고
    • Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion
    • Lang,D., Thoma,R., Henn-Sax,M., Sterner,R. and Wilmanns,M. (2000) Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion. Science, 289, 1546-1550.
    • (2000) Science , vol.289 , pp. 1546-1550
    • Lang, D.1    Thoma, R.2    Henn-Sax, M.3    Sterner, R.4    Wilmanns, M.5
  • 33
    • 0037116603 scopus 로고    scopus 로고
    • A common evolutionary origin of two elementary enzyme folds
    • Hocker,B., Schmidt,S. and Sterner,R. (2002) A common evolutionary origin of two elementary enzyme folds. FEBS Lett., 510, 133-135.
    • (2002) FEBS Lett. , vol.510 , pp. 133-135
    • Hocker, B.1    Schmidt, S.2    Sterner, R.3
  • 34
    • 0036051516 scopus 로고    scopus 로고
    • Deoxyribonucleotide synthesis in anaerobic microorganisms: The class III ribonucleotide reductase
    • Fontecave,M., Mulliez,E. and Logan,D.T. (2002) Deoxyribonucleotide synthesis in anaerobic microorganisms: the class III ribonucleotide reductase. Prog. Nucleic Acid Res. Mol. Biol., 72, 95-127.
    • (2002) Prog. Nucleic Acid Res. Mol. Biol. , vol.72 , pp. 95-127
    • Fontecave, M.1    Mulliez, E.2    Logan, D.T.3
  • 35
    • 0035823567 scopus 로고    scopus 로고
    • The anaerobic ribonucleotide reductase from Lactococcus lactis. Interactions between the two proteins NrdD and NrdG
    • Torrents,E., Eliasson,R., Wolpher,H., Graslund,A. and Reichard,P. (2001) The anaerobic ribonucleotide reductase from Lactococcus lactis. Interactions between the two proteins NrdD and NrdG. J. Biol. Chem., 276, 33488-33494.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33488-33494
    • Torrents, E.1    Eliasson, R.2    Wolpher, H.3    Graslund, A.4    Reichard, P.5
  • 36
    • 0032579314 scopus 로고    scopus 로고
    • Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C
    • Heinz,D.W., Essen,L.O. and Williams,R.L. (1998) Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C. J. Mol. Biol., 275, 635-650.
    • (1998) J. Mol. Biol. , vol.275 , pp. 635-650
    • Heinz, D.W.1    Essen, L.O.2    Williams, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.