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Title
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L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy.
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Authors
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H.R.Jonker,
S.Ilin,
S.K.Grimm,
J.Wöhnert,
H.Schwalbe.
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Ref.
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Nucleic Acids Res, 2007,
35,
441-454.
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PubMed id
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Abstract
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Ribosomal proteins are assumed to stabilize specific RNA structures and promote
compact folding of the large rRNA. The conformational dynamics of the protein
between the bound and unbound state play an important role in the binding
process. We have studied those dynamical changes in detail for the highly
conserved complex between the ribosomal protein L11 and the GTPase region of 23S
rRNA. The RNA domain is compactly folded into a well defined tertiary structure,
which is further stabilized by the association with the C-terminal domain of the
L11 protein (L11(ctd)). In addition, the N-terminal domain of L11 (L11(ntd)) is
implicated in the binding of the natural thiazole antibiotic thiostrepton, which
disrupts the elongation factor function. We have studied the conformation of the
ribosomal protein and its dynamics by NMR in the unbound state, the RNA bound
state and in the ternary complex with the RNA and thiostrepton. Our data reveal
a rearrangement of the L11(ntd), placing it closer to the RNA after binding of
thiostrepton, which may prevent binding of elongation factors. We propose a
model for the ternary L11-RNA-thiostrepton complex that is additionally based on
interaction data and conformational information of the L11 protein. The model is
consistent with earlier findings and provides an explanation for the role of
L11(ntd) in elongation factor binding.
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