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PDBsum entry 3d0x
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J Biol Chem
283:22347-22351
(2008)
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PubMed id:
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Crystal structure of the lysine riboswitch regulatory mRNA element.
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A.D.Garst,
A.Héroux,
R.P.Rambo,
R.T.Batey.
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ABSTRACT
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Riboswitches are metabolite-sensitive elements found in mRNAs that control gene
expression through a regulatory secondary structural switch. Along with
regulation of lysine biosynthetic genes, mutations within the lysine-responsive
riboswitch (L-box) play a role in the acquisition of resistance to antimicrobial
lysine analogs. To understand the structural basis for lysine binding, we have
determined the 2.8 angstroms resolution crystal structure of lysine bound to the
Thermotoga maritima asd lysine riboswitch ligand-binding domain. The structure
reveals a complex architecture scaffolding a binding pocket completely
enveloping lysine. Mutations conferring antimicrobial resistance cluster around
this site as well as highly conserved long range interactions, indicating that
they disrupt lysine binding or proper folding of the RNA. Comparison of the free
and bound forms by x-ray crystallography, small angle x-ray scattering, and
chemical probing reveals almost identical structures, indicating that lysine
induces only limited and local conformational changes upon binding.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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K.S.Keating,
and
A.M.Pyle
(2012).
RCrane: semi-automated RNA model building.
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Acta Crystallogr D Biol Crystallogr,
68,
985-995.
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A.Werner
(2011).
Predicting translational diffusion of evolutionary conserved RNA structures by the nucleotide number.
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Nucleic Acids Res,
39,
e17.
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B.Heppell,
S.Blouin,
A.M.Dussault,
J.Mulhbacher,
E.Ennifar,
J.C.Penedo,
and
D.A.Lafontaine
(2011).
Molecular insights into the ligand-controlled organization of the SAM-I riboswitch.
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Nat Chem Biol,
7,
384-392.
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S.Blouin,
R.Chinnappan,
and
D.A.Lafontaine
(2011).
Folding of the lysine riboswitch: importance of peripheral elements for transcriptional regulation.
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Nucleic Acids Res,
39,
3373-3387.
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C.D.Stoddard,
R.K.Montange,
S.P.Hennelly,
R.P.Rambo,
K.Y.Sanbonmatsu,
and
R.T.Batey
(2010).
Free state conformational sampling of the SAM-I riboswitch aptamer domain.
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Structure,
18,
787-797.
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PDB codes:
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J.E.Wedekind
(2010).
The apo riboswitch as a molecular hydra.
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Structure,
18,
757-758.
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J.M.Kelley,
and
D.Hamelberg
(2010).
Atomistic basis for the on-off signaling mechanism in SAM-II riboswitch.
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Nucleic Acids Res,
38,
1392-1400.
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J.Ouellet,
S.Melcher,
A.Iqbal,
Y.Ding,
and
D.M.Lilley
(2010).
Structure of the three-way helical junction of the hepatitis C virus IRES element.
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RNA,
16,
1597-1609.
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L.Huang,
A.Serganov,
and
D.J.Patel
(2010).
Structural insights into ligand recognition by a sensing domain of the cooperative glycine riboswitch.
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Mol Cell,
40,
774-786.
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PDB codes:
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M.Ali,
J.Lipfert,
S.Seifert,
D.Herschlag,
and
S.Doniach
(2010).
The ligand-free state of the TPP riboswitch: a partially folded RNA structure.
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J Mol Biol,
396,
153-165.
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N.J.Baird,
and
A.R.Ferré-D'Amaré
(2010).
Idiosyncratically tuned switching behavior of riboswitch aptamer domains revealed by comparative small-angle X-ray scattering analysis.
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RNA,
16,
598-609.
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R.K.Montange,
E.Mondragón,
D.van Tyne,
A.D.Garst,
P.Ceres,
and
R.T.Batey
(2010).
Discrimination between closely related cellular metabolites by the SAM-I riboswitch.
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J Mol Biol,
396,
761-772.
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PDB codes:
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R.P.Rambo,
and
J.A.Tainer
(2010).
Improving small-angle X-ray scattering data for structural analyses of the RNA world.
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RNA,
16,
638-646.
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R.P.Rambo,
and
J.A.Tainer
(2010).
Bridging the solution divide: comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering.
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Curr Opin Struct Biol,
20,
128-137.
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A.D.Garst,
and
R.T.Batey
(2009).
A switch in time: detailing the life of a riboswitch.
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Biochim Biophys Acta,
1789,
584-591.
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A.Roth,
and
R.R.Breaker
(2009).
The structural and functional diversity of metabolite-binding riboswitches.
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Annu Rev Biochem,
78,
305-334.
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A.Serganov,
L.Huang,
and
D.J.Patel
(2009).
Coenzyme recognition and gene regulation by a flavin mononucleotide riboswitch.
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Nature,
458,
233-237.
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PDB codes:
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A.Serganov
(2009).
The long and the short of riboswitches.
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Curr Opin Struct Biol,
19,
251-259.
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A.Villa,
J.Wöhnert,
and
G.Stock
(2009).
Molecular dynamics simulation study of the binding of purine bases to the aptamer domain of the guanine sensing riboswitch.
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Nucleic Acids Res,
37,
4774-4786.
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H.Fauzi,
A.Agyeman,
and
J.V.Hines
(2009).
T box transcription antitermination riboswitch: influence of nucleotide sequence and orientation on tRNA binding by the antiterminator element.
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Biochim Biophys Acta,
1789,
185-191.
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M.Naville,
and
D.Gautheret
(2009).
Transcription attenuation in bacteria: theme and variations.
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Brief Funct Genomic Proteomic,
8,
482-492.
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N.Kulshina,
N.J.Baird,
and
A.R.Ferré-D'Amaré
(2009).
Recognition of the bacterial second messenger cyclic diguanylate by its cognate riboswitch.
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Nat Struct Mol Biol,
16,
1212-1217.
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PDB code:
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S.D.Gilbert,
F.E.Reyes,
A.L.Edwards,
and
R.T.Batey
(2009).
Adaptive ligand binding by the purine riboswitch in the recognition of guanine and adenine analogs.
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Structure,
17,
857-868.
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PDB codes:
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I.Lebars,
P.Legrand,
A.Aimé,
N.Pinaud,
S.Fribourg,
and
C.Di Primo
(2008).
Exploring TAR-RNA aptamer loop-loop interaction by X-ray crystallography, UV spectroscopy and surface plasmon resonance.
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Nucleic Acids Res,
36,
7146-7156.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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