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PDBsum entry 2l1v
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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 insights into riboswitch control of the biosynthesis of queuosine, A modified nucleotide found in the anticodon of tRNA.
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Authors
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M.Kang,
R.Peterson,
J.Feigon.
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Ref.
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Mol Cell, 2009,
33,
784-790.
[DOI no: ]
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PubMed id
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Abstract
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The modified nucleotide queuosine (Q) is almost universally found in the
anticodon wobble position of specific tRNAs. In many bacteria, biosynthesis of Q
is modulated by a class of regulatory mRNA elements called riboswitches. The
preQ(1) riboswitch, found in the 5'UTR of bacterial genes involved in synthesis
of the Q precursors preQ(0) and preQ(1), contains the smallest known aptamer
domain. We report the solution structure of the preQ(1) riboswitch aptamer
domain from Bacillus subtilis bound to preQ(1), which is a unique compact
pseudoknot with three loops and two stems that encapsulates preQ(1) at the
junction between the two stems. The pseudoknot only forms in the presence of
preQ(1), and the 3' A-rich tail of the aptamer domain is an integral part of the
pseudoknot. In the absence of preQ(1), the A-rich tail forms part of the
antiterminator. These structural studies provide insight into riboswitch
transcriptional control of preQ(1) biosynthesis.
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Figure 2.
Figure 2. Structure of the Complex of the Minimal preQ[1]
Riboswitch Aptamer with preQ[1] (A) Sequence and predicted
hairpin-tail secondary structure of the preQ[1] riboswitch
aptamer 36 queC(C14,17U), with pseudoknot elements labeled.
(B) Schematic of preQ[1] riboswitch aptamer complex fold.
Hydrogen bond interactions between bases are indicated with the
notation of Leontis and Westhof (Leontis and Westhof, 2001).
(C) Stereoview of stick representation of the lowest energy
structure (nt 3–36, preQ[1]). (D) van der Waals
representations of the lowest-energy structure. Structural
elements are colored red (P1), blue (P2), orange (L1), gold
(L2), green (L3), and magenta (preQ[1]).
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Figure 3.
Figure 3. The preQ[1] Binding Pocket and the A-Amino Kissing
Motif (A) Side view of the three layers of the conserved
binding pocket showing the preQ[1] base quadruple, base triple
above, and base quadruple below shown as sticks. (B)
Close-up view of preQ[1] in the binding pocket, shown with van
der Waals surface. (C) C33-G13-A18 (P2-L2) base triple.
(D) C19-preQ[1]-A32-U9 (L2-preQ[1]-L3-L1) base quadruple.
(E) A30-G7-C20-A31 (P1-L3) base quadruple. A30 and A31 form
an A-platform and interact with the minor groove of G7-C20,
respectively. The C20 2′OH appears as an unusually lowfield
shifted resonance (9.01 ppm) in the proton spectra (see Figure
S5). (F) Interaction of L3 with the minor groove of P1. The
bases of the A-rich L3 interact primarily with their
Watson-Crick edge, forming a series of AN6H hydrogen bonds with
nucleotides of P1. (G) Interaction of A25 with G4 in P1.
(H) Interaction of A27 with A5 in P1. Color scheme is the
same as in Figure 2.
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2009,
33,
784-790)
copyright 2009.
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Headers
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