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Volumn 106, Issue 20, 2009, Pages 8180-8185

Atomic structure of a folate/FAD-dependent tRNA T54 methyltransferase

Author keywords

Modification; TrmFO; X ray crystallography

Indexed keywords

CARBENE; FLAVINE ADENINE NUCLEOTIDE; FOLIC ACID; GLUTATHIONE; HISTIDINE; IMIDAZOLE; PROTEIN; PROTEIN GIDA; PTERIDINE; QUERCETIN; TETRAHYDROFOLIC ACID; THERMUS THERMOPHILUS TRMFO; TRANSFER RNA METHYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 66349097175     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0901330106     Document Type: Article
Times cited : (57)

References (29)
  • 1
    • 0029169650 scopus 로고
    • Genetic dissection of synthesis and function of modified nucleosides In bacterial transfer RNA
    • Björk CR (1995) Genetic dissection of synthesis and function of modified nucleosides In bacterial transfer RNA, Prog Nucleic Add Res Mol Biol 50:263-338,
    • (1995) Prog Nucleic Add Res Mol Biol , vol.50 , pp. 263-338
    • Björk, C.R.1
  • 2
    • 58149191272 scopus 로고    scopus 로고
    • tRNAdb 2009: Compilation of tRNAsequences and tRNAgenes
    • Juhllng F, et al, (2009) tRNAdb 2009: Compilation of tRNAsequences and tRNAgenes, Nucleic Adds Res 37:D159-162,
    • (2009) Nucleic Adds Res , vol.37
    • Juhllng, F.1
  • 3
    • 0017133583 scopus 로고
    • CD spectra of 5-methyl-2-thlouridine in tRNA-Met-f from an extreme thermophile
    • Watanabe K, Oshima T, Nishimura S (1976) CD spectra of 5-methyl-2-thlouridine in tRNA-Met-f from an extreme thermophile, Nucleic Adds Res 3:1703-1713,
    • (1976) Nucleic Adds Res , vol.3 , pp. 1703-1713
    • Watanabe, K.1    Oshima, T.2    Nishimura, S.3
  • 4
    • 0037130958 scopus 로고    scopus 로고
    • Shigi N, Suzuki T, Tamakoshi M, Oshima T, Watanabe K (2002) Conserved bases In the TPsi C loop of tRNA are determinants for thermophile-specific 2-thiouridylation at position 54, J Biol Chem 277:39128-39135,
    • Shigi N, Suzuki T, Tamakoshi M, Oshima T, Watanabe K (2002) Conserved bases In the TPsi C loop of tRNA are determinants for thermophile-specific 2-thiouridylation at position 54, J Biol Chem 277:39128-39135,
  • 5
    • 0018974885 scopus 로고
    • Cloning and restriction mapping of the trmA gene coding for transfer ribonucleic add (5-methyluridine)- methyltransferase In Escherichia coll K-12
    • Ny T, Bj¿rk GR (1980) Cloning and restriction mapping of the trmA gene coding for transfer ribonucleic add (5-methyluridine)- methyltransferase In Escherichia coll K-12, J Bacteriol 142:371-379,
    • (1980) J Bacteriol , vol.142 , pp. 371-379
    • Ny, T.1    Bj¿rk, G.R.2
  • 6
    • 37349022099 scopus 로고    scopus 로고
    • Acquisition of a bacterial RumA-type tRNA(uracll-54, C5)-methyltransferase by Archaea through an ancient horizontal gene transfer
    • Urbonavlčlus J, et al, (2008) Acquisition of a bacterial RumA-type tRNA(uracll-54, C5)-methyltransferase by Archaea through an ancient horizontal gene transfer, Mol Microbiol 67:323-335,
    • (2008) Mol Microbiol , vol.67 , pp. 323-335
    • Urbonavlčlus, J.1
  • 9
    • 0017145150 scopus 로고
    • Biosynthesis of ribothymidine in the transfer RNAof Streptococcus faecalls and Bacilus subtilis. A methylation of RNA Involving 5,10-methylenetetrahydrofolate
    • Delk AS, Romeo JM, Nagle DP, Jr, Rabinowitz JC (1976) Biosynthesis of ribothymidine in the transfer RNAof Streptococcus faecalls and Bacilus subtilis. A methylation of RNA Involving 5,10-methylenetetrahydrofolate, J Biol Chem 251:7649-7656,
    • (1976) J Biol Chem , vol.251 , pp. 7649-7656
    • Delk, A.S.1    Romeo, J.M.2    Nagle Jr, D.P.3    Rabinowitz, J.C.4
  • 12
    • 34548740836 scopus 로고    scopus 로고
    • In vitro detection of the enzymatic activity of folate-dependent tRNA (Uracll-54,-C5)methyltransferase: Evolutionary Implications
    • Urbonavicius J, Brochier-Armanet C, Skouloubris S, Myllykallio H, Grosjean H (2007) In vitro detection of the enzymatic activity of folate-dependent tRNA (Uracll-54,-C5)methyltransferase: Evolutionary Implications, Methods Enzymol 425:103-119,
    • (2007) Methods Enzymol , vol.425 , pp. 103-119
    • Urbonavicius, J.1    Brochier-Armanet, C.2    Skouloubris, S.3    Myllykallio, H.4    Grosjean, H.5
  • 13
    • 40449104681 scopus 로고    scopus 로고
    • Cicml N (2008) Crystallization and preliminary X- raycrystallographlccharacterlzatlon of TrmFO, a folate-dependent tRNA methyltransferase from Thermotoga maritima. Acta Crystallogr F 64:193-195,
    • Cicml N (2008) Crystallization and preliminary X- raycrystallographlccharacterlzatlon of TrmFO, a folate-dependent tRNA methyltransferase from Thermotoga maritima. Acta Crystallogr F 64:193-195,
  • 14
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite version 3
    • Holm L, Kaariainen S, Rosenstrom P, Schenkel A (2008) Searching protein structure databases with DaliLite version 3, Bioinformatics 24:2780-2781,
    • (2008) Bioinformatics , vol.24 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 15
    • 44949138270 scopus 로고    scopus 로고
    • Crystal structures of the conserved tRNA-modifying enzyme GidA: Implications for Its Interaction with MnmE and substrate
    • Meyer S, Scrima A, Versees W, Wittinghofer A (2008) Crystal structures of the conserved tRNA-modifying enzyme GidA: Implications for Its Interaction with MnmE and substrate, J Mol Biol 380:532-547,
    • (2008) J Mol Biol , vol.380 , pp. 532-547
    • Meyer, S.1    Scrima, A.2    Versees, W.3    Wittinghofer, A.4
  • 16
    • 33845672606 scopus 로고    scopus 로고
    • Further insights into the tRNA modification process controlled by proteins MnmE and Gid A of Escherichia coll
    • Yim L, Moukadiri I, BjÖrk GR, Armengod ME (2006) Further insights into the tRNA modification process controlled by proteins MnmE and Gid A of Escherichia coll. Nucleic Adds Res 34:5892-5905,
    • (2006) Nucleic Adds Res , vol.34 , pp. 5892-5905
    • Yim, L.1    Moukadiri, I.2    BjÖrk, G.R.3    Armengod, M.E.4
  • 17
    • 0037457980 scopus 로고    scopus 로고
    • Lessons and conclusions from dissecting the mechanism of a bisubstrate enzyme: Thymidylate synthase mutagenesis, function, and structure
    • Finer-Moore JS, Santi DV, Stroud RM (2003) Lessons and conclusions from dissecting the mechanism of a bisubstrate enzyme: Thymidylate synthase mutagenesis, function, and structure, Biochemistry 42:248-256,
    • (2003) Biochemistry , vol.42 , pp. 248-256
    • Finer-Moore, J.S.1    Santi, D.V.2    Stroud, R.M.3
  • 18
    • 0037457982 scopus 로고    scopus 로고
    • Conformational dynamics along an enzymatic reaction pathway: Thymidylate synthase, the movie
    • Stroud RM, Finer-Moore JS (2003) Conformational dynamics along an enzymatic reaction pathway: Thymidylate synthase, "the movie," Biochemistry 42:239-247,
    • (2003) Biochemistry , vol.42 , pp. 239-247
    • Stroud, R.M.1    Finer-Moore, J.S.2
  • 19
    • 0037025191 scopus 로고    scopus 로고
    • An alternative flavin-dependent mechanism for thymidylate synthesis
    • Myllykallio H, etal, (2002) An alternative flavin-dependent mechanism for thymidylate synthesis, Science 297:105-107,
    • (2002) Science , vol.297 , pp. 105-107
    • Myllykallio, H.1
  • 20
    • 0026474956 scopus 로고
    • sU54)-methyltransferase and RNA substrates
    • sU54)-methyltransferase and RNA substrates, Biochemistry 31:10295-10302,
    • (1992) Biochemistry , vol.31 , pp. 10295-10302
    • Gu, X.1    Santi, D.V.2
  • 21
    • 2442601478 scopus 로고    scopus 로고
    • Functional evidence for active site location of tetrameric thymidylate synthase X at the Interphase of three monomers
    • Leduc D, etal, (2004) Functional evidence for active site location of tetrameric thymidylate synthase X at the Interphase of three monomers, Proc Nati Acad Sci USA 101:7252-7257,
    • (2004) Proc Nati Acad Sci USA , vol.101 , pp. 7252-7257
    • Leduc, D.1
  • 22
    • 12444261732 scopus 로고    scopus 로고
    • Direct observation of the participation of flavin in product formation by thyX-encoded thymidylate synthase
    • Gattls SG, Palfey BA (2005) Direct observation of the participation of flavin in product formation by thyX-encoded thymidylate synthase, J Am Chem Soc 127:832-833,
    • (2005) J Am Chem Soc , vol.127 , pp. 832-833
    • Gattls, S.G.1    Palfey, B.A.2
  • 23
    • 4043057882 scopus 로고    scopus 로고
    • Mechanistic studies of a flavindependent thymidylate synthase
    • Agrawal N, Lesley SA, Kuhn P, Kohen A (2004) Mechanistic studies of a flavindependent thymidylate synthase, Biochemistry 43:10295-10301,
    • (2004) Biochemistry , vol.43 , pp. 10295-10301
    • Agrawal, N.1    Lesley, S.A.2    Kuhn, P.3    Kohen, A.4
  • 24
    • 0142103146 scopus 로고    scopus 로고
    • Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein
    • Mathews II, et al, (2003) Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein, Structure (London) 11:677690.
    • (2003) Structure (London) , vol.11 , pp. 677690
    • Mathews II1
  • 25
    • 24944591878 scopus 로고    scopus 로고
    • Sampathkumar P, et al, (2005) Structure of the Mycobacterium tuberculosis flavin dependent thymldylate synthase (MtbThyX) at 2.0-Å resolution, J Mol Biol 352:10911104,
    • Sampathkumar P, et al, (2005) Structure of the Mycobacterium tuberculosis flavin dependent thymldylate synthase (MtbThyX) at 2.0-Å resolution, J Mol Biol 352:10911104,
  • 26
    • 33751239437 scopus 로고    scopus 로고
    • 1G37) methyltransferase (TrmD) from Aquifex aeollcus
    • 1G37) methyltransferase (TrmD) from Aquifex aeollcus. Genes Cells 11:1353-1365,
    • (2006) Genes Cells , vol.11 , pp. 1353-1365
    • Takeda, H.1
  • 27
    • 10344262083 scopus 로고    scopus 로고
    • 7G46) methyltransferase from Aquifex aeollcus
    • 7G46) methyltransferase from Aquifex aeollcus. J Biol Chem 279:49151-49159,
    • (2004) J Biol Chem , vol.279 , pp. 49151-49159
    • Okamoto, H.1
  • 28
    • 0028936082 scopus 로고
    • Mobilities of modified ribonucleotides on two-dimensional cellulose thin-layer chromatography
    • Keith G (1995) Mobilities of modified ribonucleotides on two-dimensional cellulose thin-layer chromatography, Biochimie 77:142-144,
    • (1995) Biochimie , vol.77 , pp. 142-144
    • Keith, G.1
  • 29
    • 0035964342 scopus 로고    scopus 로고
    • Baker NA, Sept D, Joseph S, Hoist MJ, McCammon JA (2001) Electrostatics of nanosystems: Application to microtubules and the ribosome, Proc Nati Acad Sci USA 98:1003710041,
    • Baker NA, Sept D, Joseph S, Hoist MJ, McCammon JA (2001) Electrostatics of nanosystems: Application to microtubules and the ribosome, Proc Nati Acad Sci USA 98:1003710041,


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