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Biopolym. Cell. 2026; 42(1):23-31.
http://dx.doi.org/10.7124/bc.000B30
Structure and Function of Biopolymers
Molecular dynamics of Trp40 form of B.taurus tyrosyl-tRNA synthetase with replacements of Trp87 and Trp283 by alanine
1Lozhko D. M., 1Zayets V. N., 1Kornelyuk O. I.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03143

Abstract

Aim. Analysis of conformational flexibility of mutant Trp40 form of Bos taurus Tyr-tRNA-synthetase (BtTyrRS) where single Trp was localized near active site. Methods. Computational site directed mutagenesis of Trp87 and 283 residues using the AlphaFold3 server. In silico modeling of 3D structure and molecular dynamics (MD) simulation of mini Trp40 BtTyrRS mutant form. Results. Computational modeling of Trp40 mutant BtTyrRS form has not revealed significant changes at enzyme active site. A model of 3D structure of single-tryptophan form of BtTyrRS presents a compact structure of mutant protein and rigid microenvironment of Trp40 at the active site. Conclusions. The replacement of Trp residues at positions 87 and 283 in the amino acid sequence of mini BtTyrRS with alanine residues does not affect the structure of the enzyme active site. Stable mutant single-tryptophan mini BtTyrRS protein is suitable both for fluorescence studies of structural dynamic and catalytic properties of this enzyme.
Keywords: tyrosyl-tRNA synthetase, mutant form of mini TyrRS, computational modeling, molecular dynamics
Full text: (PDF, in English)

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