Structural basis for specific, high-affinity tetracycline binding by an in vitro evolved aptamer and artificial riboswitch.

Structural basis for specific, high-affinity tetracycline binding by an in vitro evolved aptamer and artificial riboswitch.
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DOI:
10.1016/j.chembiol.2008.09.004
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发表时间:
2008-10-20
影响因子:
--
通讯作者:
Ferré-D'Amaré AR
Ferré-D'Amaré AR
中科院分区:
生物1区
文献类型:
--
作者:
Xiao H;Edwards TE;Ferré-D'Amaré AR

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The tetracycline aptamer is an in vitro selected RNA that binds to the antibiotic with the highest known affinity of an artificial RNA for a small molecule (Kd ~ 0.8 nM). It is one of few aptamers known to be capable of modulating gene expression in vivo. The 2.2 Å-resolution cocrystal structure of the aptamer reveals a pseudoknot-like fold formed by tertiary interactions between a 11-nucleotide loop and the minor groove of an irregular helix. Tetracycline binds within this interface as a magnesium ion chelate. The structure, together with previous biochemical and biophysical data, indicates that the aptamer undergoes localized folding concomitant with tetracycline binding. The three-helix junction, h-shaped architecture of this artificial RNA is more complex than those of most aptamers and is reminiscent of those of some natural riboswitches.
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