L Methionine Crystal
Mostrando 1-12 de 12 artigos, teses e dissertações.
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1. Espectroscopia Raman dos AminoÃcidos L-metionina e DL-alanina e de Nanotubos de Carbono. / Raman spectroscopy of L-methionine and DL-alananine amino acids and Carbon Nanotubes
No presente trabalho foram realizadas medidas de espalhamento Raman polarizado em cristais de L-metionina e de DL-alanina (dois aminoÃcidos) e em diversas amostras de nanotubos de carbono de parede simples (SWNT). As medidas de espalhamento Raman em cristais de L-metionina foram realizadas no intervalo espectral entre 50 cm-1 e 3100 cm-1 desde a temperatura
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 07/03/2008
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2. Crystal Structures of Alfalfa Caffeoyl Coenzyme A 3-O-Methyltransferase1
Caffeoyl coenzyme A 3-O-methyltransferases (CCoAOMTs) are S-adenosyl-l-methionine-dependent O-methyltransferases (OMTs) involved in lignin biosynthesis. Plant CCoAOMTs belong to a distinct family of OMTs, more closely related to the mammalian catechol OMTs than to other plant OMTs. The crystal structure of alfalfa (Medicago sativa) CCoAOMT in complex with th
American Society of Plant Biologists.
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3. Crystal structure of MboIIA methyltransferase
DNA methyltransferases (MTases) are sequence-specific enzymes which transfer a methyl group from S-adenosyl-l-methionine (AdoMet) to the amino group of either cytosine or adenine within a recognized DNA sequence. Methylation of a base in a specific DNA sequence protects DNA from nucleolytic cleavage by restriction enzymes recognizing the same DNA sequence. W
Oxford University Press.
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4. Crystal structure of RlmAI: Implications for understanding the 23S rRNA G745/G748-methylation at the macrolide antibiotic-binding site
The RlmA class of enzymes (RlmAI and RlmAII) catalyzes N1-methylation of a guanine base (G745 in Gram-negative and G748 in Gram-positive bacteria) of hairpin 35 of 23S rRNA. We have determined the crystal structure of Escherichia coli RlmAI at 2.8-Å resolution, providing 3D structure information for the RlmA class of RNA methyltransferases. The dimeric prot
National Academy of Sciences.
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5. The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale
The x-ray crystal structure of the pyridoxal-5′-phosphate (PLP), S-adenosyl-l-methionine (SAM), and [4Fe–4S]-dependent lysine-2,3-aminomutase (LAM) of Clostridium subterminale has been solved to 2.1-Å resolution by single-wavelength anomalous dispersion methods on a l-selenomethionine-substituted complex of LAM with [4Fe–4S]2+, PLP, SAM, and l-α-lysi
National Academy of Sciences.
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6. Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition
tRNA(m1G37)methyltransferase (TrmD) catalyzes the transfer of a methyl group from S-adenosyl-l- methionine (AdoMet) to G37 within a subset of bacterial tRNA species, which have a G residue at the 36th position. The modified guanosine is adjacent to and 3′ of the anticodon and is essential for the maintenance of the correct reading frame during translation.
Oxford University Press.
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7. An RNA cap (nucleoside-2′-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization
Viruses represent an attractive system with which to study the molecular basis of mRNA capping and its relation to the RNA transcription machinery. The RNA-dependent RNA polymerase NS5 of flaviviruses presents a characteristic motif of S-adenosyl-l-methionine-dependent methyltransferases at its N-terminus, and polymerase motifs at its C-terminus. The crystal
Oxford University Press.
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8. Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9–AdoMet
The methylation of lysine residues of histones plays a pivotal role in the regulation of chromatin structure and gene expression. Here, we report two crystal structures of SET7/9, a histone methyltransferase (HMTase) that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-l-methionine (AdoMet) determined at 1.7 and 2.3 Å resolution.
Oxford University Press.
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9. Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine.
The Thermus aquaticus DNA methyltransferase M.Taq I (EC 2.1.1.72) methylates N6 of adenine in the specific double-helical DNA sequence TCGA by transfer of --CH3 from the cofactor S-adenosyl-L-methionine. The x-ray crystal structure at 2.4-A resolution of this enzyme in complex with S-adenosylmethionine shows alpha/beta folding of the polypeptide into two dom
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10. Structure of human DNMT2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA
DNMT2 is a human protein that displays strong sequence similarities to DNA (cytosine-5)-methyltransferases (m5C MTases) of both prokaryotes and eukaryotes. DNMT2 contains all 10 sequence motifs that are conserved among m5C MTases, including the consensus S-adenosyl-l-methionine-binding motifs and the active site ProCys dipeptide. DNMT2 has close homolog
Oxford University Press.
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11. Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC′ redefines the substrate-binding site and suggests a model for protein–RNA interactions
The Erm family of adenine-N6 methyltransferases (MTases) is responsible for the development of resistance to macrolide–lincosamide–streptogramin B antibiotics through the methylation of 23S ribosomal RNA. Hence, these proteins are important potential drug targets. Despite the availability of the NMR and crystal structures of two members of the family (Er
Oxford University Press.
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12. Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment.
We have determined the structure of Pvu II methyltransferase (M. Pvu II) complexed with S -adenosyl-L-methionine (AdoMet) by multiwavelength anomalous diffraction, using a crystal of the selenomethionine-substituted protein. M. Pvu II catalyzes transfer of the methyl group from AdoMet to the exocyclic amino (N4) nitrogen of the central cytosine in its recogn