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Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition

The arginyl-tRNA synthetase (ArgRS) catalyzes the esterification reaction between L-arginine and its cognate tRNA(Arg). Previously reported structures of ArgRS shed considerable light on the tRNA recognition mechanism, while the aspect of amino acid binding in ArgRS remains largely unexplored. Here...

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Detalles Bibliográficos
Autores principales: Bi, Kelei, Zheng, Yueting, Gao, Feng, Dong, Jianshu, Wang, Jiangyun, Wang, Yi, Gong, Weimin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Higher Education Press 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3956977/
https://www.ncbi.nlm.nih.gov/pubmed/24474195
http://dx.doi.org/10.1007/s13238-013-0012-1
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author Bi, Kelei
Zheng, Yueting
Gao, Feng
Dong, Jianshu
Wang, Jiangyun
Wang, Yi
Gong, Weimin
author_facet Bi, Kelei
Zheng, Yueting
Gao, Feng
Dong, Jianshu
Wang, Jiangyun
Wang, Yi
Gong, Weimin
author_sort Bi, Kelei
collection PubMed
description The arginyl-tRNA synthetase (ArgRS) catalyzes the esterification reaction between L-arginine and its cognate tRNA(Arg). Previously reported structures of ArgRS shed considerable light on the tRNA recognition mechanism, while the aspect of amino acid binding in ArgRS remains largely unexplored. Here we report the first crystal structure of E. coli ArgRS (eArgRS) complexed with L-arginine, and a series of mutational studies using isothermal titration calorimetry (ITC). Combined with previously reported work on ArgRS, our results elucidated the structural and functional roles of a series of important residues in the active site, which furthered our understanding of this unique enzyme. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s13238-013-0012-1) contains supplementary material, which is available to authorized users.
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spelling pubmed-39569772014-03-21 Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition Bi, Kelei Zheng, Yueting Gao, Feng Dong, Jianshu Wang, Jiangyun Wang, Yi Gong, Weimin Protein Cell Research Article The arginyl-tRNA synthetase (ArgRS) catalyzes the esterification reaction between L-arginine and its cognate tRNA(Arg). Previously reported structures of ArgRS shed considerable light on the tRNA recognition mechanism, while the aspect of amino acid binding in ArgRS remains largely unexplored. Here we report the first crystal structure of E. coli ArgRS (eArgRS) complexed with L-arginine, and a series of mutational studies using isothermal titration calorimetry (ITC). Combined with previously reported work on ArgRS, our results elucidated the structural and functional roles of a series of important residues in the active site, which furthered our understanding of this unique enzyme. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s13238-013-0012-1) contains supplementary material, which is available to authorized users. Higher Education Press 2014-01-30 2014-02 /pmc/articles/PMC3956977/ /pubmed/24474195 http://dx.doi.org/10.1007/s13238-013-0012-1 Text en © The Author(s) 2014 https://creativecommons.org/licenses/by/2.0/Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Research Article
Bi, Kelei
Zheng, Yueting
Gao, Feng
Dong, Jianshu
Wang, Jiangyun
Wang, Yi
Gong, Weimin
Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition
title Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition
title_full Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition
title_fullStr Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition
title_full_unstemmed Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition
title_short Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition
title_sort crystal structure of e. coli arginyl-trna synthetase and ligand binding studies revealed key residues in arginine recognition
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3956977/
https://www.ncbi.nlm.nih.gov/pubmed/24474195
http://dx.doi.org/10.1007/s13238-013-0012-1
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