The N-terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase (TyrRS_apm) is a monomer in solution

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• 作者：Aparajita Choudhury ; Rajat Banerjee ; ^{rbbcgc@gmail.com}
• 关键词：TyrRSapm ; Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase ; ¦¤TyrRSapm ; N-terminal domain of Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase ; aa ; amino acid ; AUC ; analytical ultracentrifuge ; DTNB ; 5 ; 5&prime ; -dithio-bis(2-nitrobenzoic acid
• 刊名：FEBS Letters
• 出版年：2013
• 出版时间：18 March, 2013
• 年：2013
• 卷：587
• 期：6
• 页码：590-599
• 全文大小：1145 K

文摘

Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase (TyrRS_apm) was the first reported aminoacyl-tRNA synthetase of viral origin. The previous crystal structure of TyrRS_apm showed a non-canonical orientation of the dimer conformation and the CP1 domain, responsible for dimer formation, displays a major modification of a motif structurally conserved in other TyrRS structures. An earlier study reported that Bacillus stearothermophilus N-terminal TyrRS exists as a dimer under native conditions. N-terminal TyrRS_apm (¦¤TyrRS_apm, 1-234 aa) was constructed to remove the C-terminal anticodon-binding domain. Here we show by Ferguson plot analysis and analytical ultracentrifugation that ¦¤TyrRS_apm exists as a monomer and contains a disulfide-bridge. The ¦¤TyrRS_apm loses the ability to bind tRNA^Tyr, however it remains active in pyrophosphate exchange with similar ligand dissociation constants as the full-length enzyme.

Structured summary of protein interactions

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