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- W2077514275 abstract "The existence of three types of phenylalanyl-tRNA synthetase (PheRS), bacterial (alphabeta)(2), eukaryotic/archaeal cytosolic (alphabeta)(2), and mitochondrial alpha, is a prominent example of structural diversity within the aaRS family. PheRSs have considerably diverged in primary sequences, domain compositions, and subunit organizations. Loss of the anticodon-binding domain B8 in human cytosolic PheRS (hcPheRS) is indicative of variations in the tRNA(Phe) binding and recognition as compared to bacterial PheRSs. We report herein the crystal structure of hcPheRS in complex with phenylalanine at 3.3 A resolution. A novel structural module has been revealed at the N terminus of the alpha subunit. It stretches out into the solvent of approximately 80 A and is made up of three structural domains (DBDs) possessing DNA-binding fold. The dramatic reduction of aminoacylation activity for truncated N terminus variants coupled with structural data and tRNA-docking model testify that DBDs play crucial role in hcPheRS activity." @default.
- W2077514275 created "2016-06-24" @default.
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- W2077514275 date "2010-03-01" @default.
- W2077514275 modified "2023-10-16" @default.
- W2077514275 title "Structure of Human Cytosolic Phenylalanyl-tRNA Synthetase: Evidence for Kingdom-Specific Design of the Active Sites and tRNA Binding Patterns" @default.
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- W2077514275 doi "https://doi.org/10.1016/j.str.2010.01.002" @default.
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