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Structure of the L1 protuberance in the ribosome.

Nikulin, A; Eliseikina, I; Tishchenko, S; Nevskaya, N; Davydova, N; Platonova, O; Piendl, W; Selmer, Maria LU ; Liljas, Anders LU and Drygin, D, et al. (2003) In Nature Structural & Molecular Biology 10(2). p.104-108
Abstract
The L1 protuberance of the 50S ribosomal subunit is implicated in the release/disposal of deacylated tRNA from the E site. The apparent mobility of this ribosomal region has thus far prevented an accurate determination of its three-dimensional structure within either the 50S subunit or the 70S ribosome. Here we report the crystal structure at 2.65 Å resolution of ribosomal protein L1 from Sulfolobus acidocaldarius in complex with a specific 55-nucleotide fragment of 23S rRNA from Thermus thermophilus. This structure fills a major gap in current models of the 50S ribosomal subunit. The conformations of L1 and of the rRNA fragment differ dramatically from those within the crystallographic model of the T. thermophilus 70S ribosome.... (More)
The L1 protuberance of the 50S ribosomal subunit is implicated in the release/disposal of deacylated tRNA from the E site. The apparent mobility of this ribosomal region has thus far prevented an accurate determination of its three-dimensional structure within either the 50S subunit or the 70S ribosome. Here we report the crystal structure at 2.65 Å resolution of ribosomal protein L1 from Sulfolobus acidocaldarius in complex with a specific 55-nucleotide fragment of 23S rRNA from Thermus thermophilus. This structure fills a major gap in current models of the 50S ribosomal subunit. The conformations of L1 and of the rRNA fragment differ dramatically from those within the crystallographic model of the T. thermophilus 70S ribosome. Incorporation of the L1–rRNA complex into the structural models of the T. thermophilus 70S ribosome and the Deinococcus radiodurans 50S subunit gives a reliable representation of most of the L1 protuberance within the ribosome. (Less)
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Nature Structural & Molecular Biology
volume
10
issue
2
pages
104 - 108
publisher
Nature Publishing Group
external identifiers
  • pmid:12514741
  • wos:000180686600011
  • scopus:0037312936
ISSN
1545-9985
DOI
10.1038/nsb886
language
English
LU publication?
yes
id
061a1cda-2cb6-45bf-acde-85663a129fab (old id 128506)
date added to LUP
2007-07-09 16:05:26
date last changed
2018-01-07 08:52:45
@article{061a1cda-2cb6-45bf-acde-85663a129fab,
  abstract     = {The L1 protuberance of the 50S ribosomal subunit is implicated in the release/disposal of deacylated tRNA from the E site. The apparent mobility of this ribosomal region has thus far prevented an accurate determination of its three-dimensional structure within either the 50S subunit or the 70S ribosome. Here we report the crystal structure at 2.65 Å resolution of ribosomal protein L1 from Sulfolobus acidocaldarius in complex with a specific 55-nucleotide fragment of 23S rRNA from Thermus thermophilus. This structure fills a major gap in current models of the 50S ribosomal subunit. The conformations of L1 and of the rRNA fragment differ dramatically from those within the crystallographic model of the T. thermophilus 70S ribosome. Incorporation of the L1–rRNA complex into the structural models of the T. thermophilus 70S ribosome and the Deinococcus radiodurans 50S subunit gives a reliable representation of most of the L1 protuberance within the ribosome.},
  author       = {Nikulin, A and Eliseikina, I and Tishchenko, S and Nevskaya, N and Davydova, N and Platonova, O and Piendl, W and Selmer, Maria and Liljas, Anders and Drygin, D and Zimmermann, R and Garber, M and Nikonov, S},
  issn         = {1545-9985},
  language     = {eng},
  number       = {2},
  pages        = {104--108},
  publisher    = {Nature Publishing Group},
  series       = {Nature Structural & Molecular Biology},
  title        = {Structure of the L1 protuberance in the ribosome.},
  url          = {http://dx.doi.org/10.1038/nsb886},
  volume       = {10},
  year         = {2003},
}