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Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB.

Selmer, Maria LU and Su, Xiao-Dong LU (2002) In EMBO Journal 21(15). p.4145-4153
Abstract
SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). We present the crystal structure of a C-terminal fragment of SelB (SelB-C) from Moorella thermoacetica at 2.12 A resolution, solved by a combination of selenium and yttrium multiwavelength anomalous dispersion. This 264 amino acid fragment contains the entire C-terminal extension beginning after the EF-Tu-homologous domains. SelB-C consists of four similar winged-helix domains arranged into the... (More)
SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). We present the crystal structure of a C-terminal fragment of SelB (SelB-C) from Moorella thermoacetica at 2.12 A resolution, solved by a combination of selenium and yttrium multiwavelength anomalous dispersion. This 264 amino acid fragment contains the entire C-terminal extension beginning after the EF-Tu-homologous domains. SelB-C consists of four similar winged-helix domains arranged into the shape of an L. This is the first example of winged-helix domains involved in RNA binding. The location of conserved basic amino acids, together with data from the literature, define the position of the mRNA-binding site. Steric requirements indicate that a conformational change may occur upon ribosome interaction. Struc tural observations and data in the literature suggest that this change happens upon mRNA binding. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
EMBO Journal
volume
21
issue
15
pages
4145 - 4153
publisher
Oxford University Press
external identifiers
  • pmid:12145214
  • wos:000177470700022
  • scopus:0036682596
ISSN
1460-2075
DOI
10.1093/emboj/cdf408
language
English
LU publication?
yes
id
ffdec5d0-b96c-4f1e-a69a-5bb10322afe8 (old id 109643)
date added to LUP
2007-07-09 16:23:52
date last changed
2017-08-27 05:41:01
@article{ffdec5d0-b96c-4f1e-a69a-5bb10322afe8,
  abstract     = {SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). We present the crystal structure of a C-terminal fragment of SelB (SelB-C) from Moorella thermoacetica at 2.12 A resolution, solved by a combination of selenium and yttrium multiwavelength anomalous dispersion. This 264 amino acid fragment contains the entire C-terminal extension beginning after the EF-Tu-homologous domains. SelB-C consists of four similar winged-helix domains arranged into the shape of an L. This is the first example of winged-helix domains involved in RNA binding. The location of conserved basic amino acids, together with data from the literature, define the position of the mRNA-binding site. Steric requirements indicate that a conformational change may occur upon ribosome interaction. Struc tural observations and data in the literature suggest that this change happens upon mRNA binding.},
  author       = {Selmer, Maria and Su, Xiao-Dong},
  issn         = {1460-2075},
  language     = {eng},
  number       = {15},
  pages        = {4145--4153},
  publisher    = {Oxford University Press},
  series       = {EMBO Journal},
  title        = {Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB.},
  url          = {http://dx.doi.org/10.1093/emboj/cdf408},
  volume       = {21},
  year         = {2002},
}