Homology modeling of structure of NH₂-terminal module of mammalian (Bos taurus) tyrosyl-tRNA synthetase

• Datum: 2002
• Hauptverfasser: Odynets, K.A., Bazylevskyi, O.E., Kornelyuk, A.I.
• Format: Artikel
• Sprache: English
• Veröffentlicht: Інститут молекулярної біології і генетики НАН України 2002
• Schriftenreihe: Біополімери і клітина
• Schlagworte: Короткі повідомлення
• Online Zugang: https://nasplib.isofts.kiev.ua/handle/123456789/156315
• Назва журналу: Digital Library of Periodicals of National Academy of Sciences of Ukraine
• Zitieren: Homology modeling of structure of NH2-terminal module of mammalian (Bos taurus) tyrosyl-tRNA synthetase / K.A. Odynets, O.E. Bazylevskyi, A.I. Kornelyuk // Вiopolymers and Cell. — 2002. — Т. 18, № 6. — С. 547-550. — Бібліогр.: 18 назв. — англ.

Mammalian tyrosyl-tRNA synthetase (TyrRS) is composed of two structural modules: the NH2-terminal catalytic core and cytokine-like COOH-terminal module. In order to elucidate the structural bases for the N-module functions we have used the computational prediction of its three-dimensional (3D) structure by comparative modeling approach. A model of the bovine TyrRS N-module represents the Rossmann nucleotide-binding fold (RF) which is linked to the α-helical domain (αHD). The RF domain forms a single β-sheet containing 5 parallel and one attached antiparallel β-strands surrounded by α-helices. The connective polypeptide, CP1, inserted between β3- and β4-strands of the RF domain is perturbed from the domain core. Comparative analysis of this multiple sequence alignment of known TyrRSs and the obtained model structure reveals the conservative surface elements, which could potentially form the tRNATyr-binding surface. This putative surface includes some exposed amino acid residues of CP1, e. g. essential Lys146 and Lys147 residues, which were identified earlier by site-directed mutagenesis.