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• W2012247656 endingPage "297" @default.
• W2012247656 startingPage "287" @default.
• W2012247656 abstract "The crystal structure of a deletion mutant of tyrosyl-tRNA synthetase from Bacillus stearothermophilus has been determined at 2.5 Å resolution using molecular replacement techniques. The genetically engineered molecule catalyses the activation of tyrosine with kinetic properties similar to those of the wild-type enzyme but no longer binds tRNATyr. It contains 319 residues corresponding to the region of the polypeptide chain for which interpretable electron density is present in crystals of the wild-type enzyme. The partly refined model of the wild-type enzyme was used as a starting point in determining the structure of the truncated mutant. The new crystals are of space group P21 and contain the molecular dimer within the asymmetric unit. The refined model has a crystallographic R-factor of 18.7% for all reflections between 8 and 2.5 Å. Each subunit contains two structural domains: the αβ domain (residues 1 to 220) containing a six-stranded β-sheet and the α-helical domain (residues 248 to 319) containing five helices. The αβ domains are related by a non-crystallographic dyad while the α-helical domains are in slightly different orientations in the two subunits. The tyrosine substrate binds in a slot at the bottom of a deep active site cleft in the middle of the αβ domain. It is surrounded by polar side-chains and water molecules that are involved in an intricate hydrogen bonding network. Both the α-amino and hydroxyl groups of the substrate make good hydrogen bonds with the protein. The amino group forms hydrogen bonds with Tyrl69-OH, Asp78-OD1 and Gln173-OE1. The phenolic hydroxyl group forms hydrogen bonds with Asp76-OD1 and Tyr34-OH. In contrast, the substrate carboxyl group makes no direct interactions with the enzyme. The results of both substrate inhibition studies and site-directed mutagenesis experiments have been examined in the light of the refined structure." @default.
• W2012247656 created "2016-06-24" @default.
• W2012247656 creator A5076997623 @default.
• W2012247656 creator A5085120671 @default.
• W2012247656 date "1987-03-01" @default.
• W2012247656 modified "2023-09-23" @default.
• W2012247656 title "Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosine" @default.
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• W2012247656 doi "https://doi.org/10.1016/0022-2836(87)90376-7" @default.
• W2012247656 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3612807" @default.
• W2012247656 hasPublicationYear "1987" @default.
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