The crystal structure of unmodified tRNA(Phe) from Escherichia coli

Post-transcriptional nucleoside modifications fine-tune the biophysical and biochemical properties of transfer RNA (tRNA) so that it is optimized for participation in cellular processes. Here we report the crystal structure of unmodified tRNA(Phe) from Escherichia coli at a resolution of 3 Å. We sho...

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Detalles Bibliográficos
Autores principales: Byrne, Robert T., Konevega, Andrey L., Rodnina, Marina V., Antson, Alfred A.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2010
Materias:
Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2896525/
https://www.ncbi.nlm.nih.gov/pubmed/20203084
http://dx.doi.org/10.1093/nar/gkq133
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author Byrne, Robert T.
Konevega, Andrey L.
Rodnina, Marina V.
Antson, Alfred A.
author_facet Byrne, Robert T.
Konevega, Andrey L.
Rodnina, Marina V.
Antson, Alfred A.
author_sort Byrne, Robert T.
collection PubMed
description Post-transcriptional nucleoside modifications fine-tune the biophysical and biochemical properties of transfer RNA (tRNA) so that it is optimized for participation in cellular processes. Here we report the crystal structure of unmodified tRNA(Phe) from Escherichia coli at a resolution of 3 Å. We show that in the absence of modifications the overall fold of the tRNA is essentially the same as that of mature tRNA. However, there are a number of significant structural differences, such as rearrangements in a triplet base pair and a widened angle between the acceptor and anticodon stems. Contrary to previous observations, the anticodon adopts the same conformation as seen in mature tRNA.
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spelling pubmed-28965252010-07-06 The crystal structure of unmodified tRNA(Phe) from Escherichia coli Byrne, Robert T. Konevega, Andrey L. Rodnina, Marina V. Antson, Alfred A. Nucleic Acids Res Structural Biology Post-transcriptional nucleoside modifications fine-tune the biophysical and biochemical properties of transfer RNA (tRNA) so that it is optimized for participation in cellular processes. Here we report the crystal structure of unmodified tRNA(Phe) from Escherichia coli at a resolution of 3 Å. We show that in the absence of modifications the overall fold of the tRNA is essentially the same as that of mature tRNA. However, there are a number of significant structural differences, such as rearrangements in a triplet base pair and a widened angle between the acceptor and anticodon stems. Contrary to previous observations, the anticodon adopts the same conformation as seen in mature tRNA. Oxford University Press 2010-07 2010-03-04 /pmc/articles/PMC2896525/ /pubmed/20203084 http://dx.doi.org/10.1093/nar/gkq133 Text en © The Author(s) 2010. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Structural Biology
Byrne, Robert T.
Konevega, Andrey L.
Rodnina, Marina V.
Antson, Alfred A.
The crystal structure of unmodified tRNA(Phe) from Escherichia coli
title The crystal structure of unmodified tRNA(Phe) from Escherichia coli
title_full The crystal structure of unmodified tRNA(Phe) from Escherichia coli
title_fullStr The crystal structure of unmodified tRNA(Phe) from Escherichia coli
title_full_unstemmed The crystal structure of unmodified tRNA(Phe) from Escherichia coli
title_short The crystal structure of unmodified tRNA(Phe) from Escherichia coli
title_sort crystal structure of unmodified trna(phe) from escherichia coli
topic Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2896525/
https://www.ncbi.nlm.nih.gov/pubmed/20203084
http://dx.doi.org/10.1093/nar/gkq133
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