Research Topics
| Nina MoorSummaryAffiliation: Institute of Chemical Biology and Fundamental Medicine Country: Russia Publications
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Detail Information
Publications
Affinity modification of phenylalanyl-tRNA synthetase from Thermus thermophilus by tRNAPhe transcripts containing 4-thiouridineN A Moor
Novosibirsk Institute of Bioorganic Chemistry, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, 630090, Russia
Biochemistry (Mosc) 63:1044-50. 1998..The prevalence of modification of the alpha-subunit suggests that tRNA has contacts with the enzyme, which have not been deciphered previously by X-ray analysis...
Localization of the binding site for the 3'-terminal sequence of tRNAPhe in subunits of phenylalanyl-tRNA synthetase from Thermus thermophilusN A Moor
Novosibirsk Institute of Bioorganic Chemistry, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, 630090, Russia
Biochemistry (Mosc) 63:1051-6. 1998..These data suggest that the nucleotide found at position 75 of tRNAPhe interacts with the beta-subunit of phenylalanyl-tRNA synthetase...
Determination of tRNA(Phe) nucleotides contacting the subunits of Thermus thermophilus phenylalanyl-tRNA synthetase by photoaffinity crosslinkingN A Moor
Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences, Novosibirsk 630090, Russia
Biochim Biophys Acta 1518:226-36. 2001..The data of independent biochemical approaches strongly suggest conformational flexibility of the complex under functional conditions, thus reflecting the importance of macromolecular dynamics for the interaction...
Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA endNina Moor
Novosibirsk Institute of Bioorganic Chemistry, 630090 Novosibirsk, Russia
Biochemistry 42:10697-708. 2003....
The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyl-adenylate analogue reveals a conformational switch of the CCA endNina Moor
Institute of Chemical Biology and Fundamental Medicine, 630090 Novosibirsk, Russia
Biochemistry 45:10572-83. 2006..Our data suggest that the idiosyncratic feature of PheRS, which aminoacylates the 2'-OH group of the terminal ribose, is dictated by the system-specific topology of the CCA end-binding site...
Bacterial and eukaryotic phenylalanyl-tRNA synthetases catalyze misaminoacylation of tRNA(Phe) with 3,4-dihydroxy-L-phenylalanineNina Moor
Institute of Chemical Biology and Fundamental Medicine, 630090 Novosibirsk, Russia
Chem Biol 18:1221-9. 2011..However, editing activity of PheRS does not guarantee reduction of the aminoacylation error rate to escape misincorporation of L-dopa into polypeptide chains...
Cloning and expression of human phenylalanyl-tRNA synthetase in Escherichia coli: comparative study of purified recombinant enzymesNina Moor
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel
Protein Expr Purif 24:260-7. 2002..coli is five times higher...
Purification, crystallization and preliminary X-ray characterization of a human mitochondrial phenylalanyl-tRNA synthetaseInna Levin
Department of Structural Biology, Weizmann Institute of Science, 76100 Rehovot, Israel
Acta Crystallogr Sect F Struct Biol Cryst Commun 63:761-4. 2007..The crystals diffracted to 2.2 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 55, b = 90, c = 96 A...
The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetaseLiron Klipcan
Department of Structural Biology, Weizmann Institute of Science, 76100 Rehovot, Israel
Structure 16:1095-104. 2008..Thus, formation of the PheRS-tRNAPhe complex in human mitochondria must be accompanied by considerable rearrangement (hinge-type rotation through approximately 160 degrees) of the ABD upon tRNA binding...
Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetaseOlga Kotik-Kogan
Department of Structural Biology, Weizmann Institute of Science, 76100 Rehovot, Israel
Structure 13:1799-807. 2005..Both structural data and tyrosine-dependent ATP hydrolysis enhanced by tRNA(Phe) provide evidence for a preferential posttransfer editing pathway in the phenylalanine-specific system...
