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PDBsum entry 2ply
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Translation/RNA
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PDB id
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2ply
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Contents |
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 _NA
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 _MG
×17
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_CL
×4
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 _CA
×2
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References listed in PDB file
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Key reference
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Title
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Structural insight into a molecular switch in tandem winged-Helix motifs from elongation factor selb.
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Authors
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N.Soler,
D.Fourmy,
S.Yoshizawa.
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Ref.
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J Mol Biol, 2007,
370,
728-741.
[DOI no: ]
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PubMed id
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Abstract
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Elongation factor SelB is responsible for co-translational incorporation of
selenocysteine (Sec) into proteins. The UGA stop codon is recoded as a Sec codon
in the presence of a downstream mRNA hairpin. In prokaryotes, in addition to the
EF-Tu-like N-terminal domains, a C-terminal extension containing four tandem
winged-helix motifs (WH1-4) recognizes the mRNA hairpin. The 2.3-A resolution
crystal structure of the Escherichia coli WH3/4 domains bound to mRNA with
mutagenesis data reveal that the two WH motifs use the same structural elements
to bind RNA. The structure together with the 2.6-A resolution structure of the
WH1-4 domains from Moorella thermoacetica bound to RNA revealed that a salt
bridge connecting WH2 to WH3 modules is disrupted upon mRNA binding. The results
provide a structural basis for the molecular switch that may allow communication
between tRNA and mRNA binding sites and illustrate how RNA acts as an activator
of the switch. The structures show that tandem WH motifs not only provide an
excellent scaffold for RNA binding but can also have an active role in the
function of protein-RNA complexes.
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Figure 1.
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Figure 6.
Figure 6. Comparison of protein–RNA interactions in the
SelB WH–RNA complexes with other nucleic acid–WH complexes.
The WH motifs are in the same orientation. (a) Protein–RNA
recognition in the E. coli WH4–SECIS RNA complex. The
N-terminal regions of helices H2 and H3 and β strands that
interact with the RNA hairpin are in red. (b) Protein–RNA
recognition in crystal contacts within the M. thermoacetica
WH2–SECIS RNA complex. The connecting loop between helix H1
and strand S1 is in red. (c) Protein–RNA recognition in
crystal contacts within the M. thermoacetica WH3–SECIS RNA
complex. The helix H3 is colored red. (d) Protein–RNA
recognition in the La NTD–RNA complex (PDB code 1ZH5). Only
the WH La motif is shown. The UUU[OH]3′ end segment is
targeted by the C-terminal region of helix H1 and insertion
helices H2 and H4 (in red). (e) The recognition helix of the WH
motif in the Sap-1 protein–DNA complex (PDB code 1bc8,^54) is
in red.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2007,
370,
728-741)
copyright 2007.
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray analysis of the mRNA-Binding domain of elongation factor selb from escherichia coli in complex with RNA.
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Authors
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N.Soler,
D.Fourmy,
S.Yoshizawa.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007,
63,
419-421.
[DOI no: ]
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PubMed id
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Figure 2.
Crystals of the SelB-WH3/4 --SECIS RNA complex in a hanging
drop. Crystal dimensions are 40 x 40 x 200 [micro]m. Acta
Crystallogr Sect F Struct Biol Cryst Commun. 2007 May 1; 63(Pt
5): 419–421. Published online 2007 April 20. doi:
10.1107/S174430910701723X. Copyright [copyright] International
Union of Crystallography 2007
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Figure 3.
X-ray diffraction image of a SelB-WH3/4 --SECIS RNA complex
crystal. The detector edge corresponds to 1.95 A resolution. The
exposure time was 30 s, the detector distance was 150 mm and the
oscillation range per frame was 1[deg]. Acta Crystallogr Sect F
Struct Biol Cryst Commun. 2007 May 1; 63(Pt 5): 419–421.
Published online 2007 April 20. doi: 10.1107/S174430910701723X.
Copyright [copyright] International Union of Crystallography
2007
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The above figures are
reproduced from the cited reference
which is an Open Access publication published by the IUCr
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