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Cristallogenèse et études structurales appliquées aux aminoacyl-ARNt synthétases

Abstract : Glutaminyl-tRNA synthetase from Deinococcus radiodurans (GlnRS-Dr) distinguishes from known GlnRSs by the presence additional long insertions. A C-terminal extension (C-ter) is predicted to adopt the same fold as part of an amidotransferase (AdT) subunit making this GlnRS almost unique among its homologs since it corresponds to the fusion of protein domains from both direct and indirect pathways of tRNA aminoacylation. In the crystal structure of GlnRS-Dr, C-ter was not solved although the unit cell was large enough to accommodate it. In the same time, NMR analysis of the extension confirmed the presence of a well structured region.
Additional structures were solved in the presence of small substrates (glutamine, 2 adenylate analogs) and the C-terminal truncated form as well. In 2 cases, it leads to the stabilization of an insertion loop closing the active site. Structure analysis, functional implication, crystal packing and plasticity properties are discussed.
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Contributor : Isabelle Martin <>
Submitted on : Thursday, January 17, 2008 - 11:18:30 AM
Last modification on : Thursday, April 23, 2020 - 2:26:32 PM
Long-term archiving on: : Friday, November 25, 2016 - 7:30:21 PM


  • HAL Id : tel-00206952, version 1



Elodie Touzé. Cristallogenèse et études structurales appliquées aux aminoacyl-ARNt synthétases. Biochimie [q-bio.BM]. Université Louis Pasteur - Strasbourg I, 2007. Français. ⟨tel-00206952⟩



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