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The N-terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase (TyrRSapm) is a monomer in solution
A CHOUDHURY,
Published in -
2013
Volume: 587
   
Issue: 6
Pages: 590 - 599
Abstract
Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase (TyrRS apm) was the first reported aminoacyl-tRNA synthetase of viral origin. The previous crystal structure of TyrRSapm 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 TyrRSapm (ΔTyrRSapm, 1-234 aa) was constructed to remove the C-terminal anticodon-binding domain. Here we show by Ferguson plot analysis and analytical ultracentrifugation that ΔTyrRSapm exists as a monomer and contains a disulfide-bridge. The ΔTyrRSapm loses the ability to bind tRNATyr, however it remains active in pyrophosphate exchange with similar ligand dissociation constants as the full-length enzyme. Structured summary of protein interactions: TyrRSapm and TyrRSapm bind by cosedimentation in solution (View interaction) TyrRSapm and TyrRSapm bind by blue native page (View interaction)TyrRSapm and TyrRSapm bind by fluorescence technology (View interaction) TyrRSapm and TyrRSapm bind by fluorescence technology (View interaction). © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
About the journal
JournalFEBS Letters
Publisher-
ISSN0014-5793