Zobrazeno 1 - 10
of 53
pro vyhledávání: '"V.N. Ankilova"'
Autor:
N. A. Moor, Inna A. Vasil'eva, Olga I. Lavrik, Maria V. Sukhanova, V.N. Ankilova, Victor G. Stepanov
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1386:1-15
It was confirmed unambiguously that the anomalously high plateau in the tRNA aminoacylation reaction catalyzed by Thermus thermophilus phenylalanyl-tRNA synthetase is a result of enzymatic synthesis of tRNA bearing two bound phenylalanyl residues (bi
Autor:
Mark Safro, Dino Moras, Maia Chernaya, Ludmila Reshetnikova, Jean-Cloud Thierry, Marc Delarue, Olga I. Lavrik, V.N. Ankilova
Publikováno v:
European Journal of Biochemistry. 208:411-417
The three-dimensional structure of the heterodimeric alpha 2 beta 2 enzyme phenylalanyl-tRNA synthetase from Thermus thermophilus HB8 has been determined by X-ray crystallography, using the multiple-isomorphous-replacement method at 0.6 nm resolution
Publikováno v:
Journal of molecular recognition : JMR. 15(4)
The extent of tRNA recognition at the level of binding by Thermus thermophilus phenylalanyl-tRNA synthetase (PheRS), one of the most complex class II synthetases, has been studied by independent measurements of the enzyme association with wild-type a
Autor:
Mark Safro, Ludmila Reshetnikova, Svetlana N. Khodyreva, Olga I. Lavrik, V.N. Ankilova, F. Frolow
Publikováno v:
Journal of Molecular Biology. 231:927-929
Phenylalanyl-tRNA synthetase (EC 6.1.1.20) from the extreme thermophile Thermus thermophilus HB8 has been crystallized with its cognate tRNA. Compared with the native crystals, the crystals of the complex are more stable to radiation damage and diffr
Publikováno v:
Biochimica et biophysica acta. 1518(3)
The nucleotides of tRNA(Phe) interacting with the subunits of Thermus thermophilus phenylalanyl-tRNA synthetase (the alpha(2)beta(2) heterotetramer) have been determined by photoaffinity crosslinking of randomly s(4)U-monosubstituted tRNA(Phe) transc
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 57(Pt 11)
The crystal structure of phenylalanyl-tRNA synthetase (PheRS) from Thermus thermophilus, a class II aminoacyl-tRNA synthetase, complexed with phenylalanyl-adenylate (Phe-AMP) was determined at 2.6 A resolution. Crystals of native PheRS were soaked in
Publikováno v:
Biochemical and biophysical research communications. 255(3)
Unlike the catalytic alpha-subunit, the beta-subunit of heterodimeric (alphabeta)2 phenylalanyl-tRNA synthetase (PheRS) has no invariant functional amino acids directly involved in the aminoacylation process as it is evident from the crystal structur
Publikováno v:
European journal of biochemistry. 234(3)
The tRNA(Phe) nucleotides required for recognition by phenylalanyl-tRNA synthetase of Thermus thermophilus have been determined using Escherichia coli tRNA(Phe) transcripts with various mutations. The anticodon nucleotides are shown to be the most im
Publikováno v:
FEBS letters. 311(3)
Phenylalanyl-tRNA synthetase from the extreme thermophilic bacterium Thermus thermophilus can incorporate more than one molecule of phenylalanine into the tRNA Phe . It is shown that the ‘hyperaminoncylated’ tRNAP Phe is the bis-2′,3′- O -phe
Publikováno v:
Biochimie. 74(4)
The tRNA Phe recognition nucleotides for phenylalanyl-tRNA synthetase from an extreme thermophile Thermus thermophilus were investigated. Using yeast tRNA Phe T7 transcripts with various point mutations it was shown that four recognition points (G34,