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PDBsum entry 1cql
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Rna
5:1419-1429
(1999)
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PubMed id:
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Structure of the phylogenetically most conserved domain of SRP RNA.
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U.Schmitz,
S.Behrens,
D.M.Freymann,
R.J.Keenan,
P.Lukavsky,
P.Walter,
T.L.James.
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ABSTRACT
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The signal recognition particle (SRP) is a phylogenetically conserved
ribonucleoprotein required for cotranslational targeting of proteins to the
membrane of the endoplasmic reticulum of the bacterial plasma membrane. Domain
IV of SRP RNA consists of a short stem-loop structure with two internal loops
that contain the most conserved nucleotides of the molecule. All known essential
interactions of SRP occur in that moiety containing domain IV. The solution
structure of a 43-nt RNA comprising the complete Escherichia coli domain IV was
determined by multidimensional NMR and restrained molecular dynamics refinement.
Our data confirm the previously determined rigid structure of a smaller
subfragment containing the most conserved, symmetric internal loop A (Schmitz et
al., Nat Struct Biol, 1999, 6:634-638), where all conserved nucleotides are
involved in nucleotide-specific structural interactions. Asymmetric internal
loop B provides a hinge in the RNA molecule; it is partially flexible, yet also
uniquely structured. The longer strand of internal loop B extends the major
groove by creating a ledge-like arrangement; for loop B however, there is no
obvious structural role for the conserved nucleotides. The structure of domain
IV suggests that loop A is the initial site for the RNA/protein interaction
creating specificity, whereas loop B provides a secondary interaction site.
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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.Wild,
G.Bange,
G.Bozkurt,
B.Segnitz,
A.Hendricks,
and
I.Sinning
(2010).
Structural insights into the assembly of the human and archaeal signal recognition particles.
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Acta Crystallogr D Biol Crystallogr,
66,
295-303.
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PDB codes:
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M.de la Peña,
D.Dufour,
and
J.Gallego
(2009).
Three-way RNA junctions with remote tertiary contacts: a recurrent and highly versatile fold.
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RNA,
15,
1949-1964.
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S.Fulle,
and
H.Gohlke
(2008).
Analyzing the flexibility of RNA structures by constraint counting.
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Biophys J,
94,
4202-4219.
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C.V.Nicchitta,
R.S.Lerner,
S.B.Stephens,
R.D.Dodd,
and
B.Pyhtila
(2005).
Pathways for compartmentalizing protein synthesis in eukaryotic cells: the template-partitioning model.
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Biochem Cell Biol,
83,
687-695.
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T.Hainzl,
S.Huang,
and
A.E.Sauer-Eriksson
(2005).
Structural insights into SRP RNA: an induced fit mechanism for SRP assembly.
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RNA,
11,
1043-1050.
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PDB code:
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M.B.Sagar,
L.Lucast,
and
J.A.Doudna
(2004).
Conserved but nonessential interaction of SRP RNA with translation factor EF-G.
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RNA,
10,
772-778.
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P.S.Klosterman,
D.K.Hendrix,
M.Tamura,
S.R.Holbrook,
and
S.E.Brenner
(2004).
Three-dimensional motifs from the SCOR, structural classification of RNA database: extruded strands, base triples, tetraloops and U-turns.
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Nucleic Acids Res,
32,
2342-2352.
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S.Baba,
M.Kajikawa,
N.Okada,
and
G.Kawai
(2004).
Solution structure of an RNA stem-loop derived from the 3' conserved region of eel LINE UnaL2.
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RNA,
10,
1380-1387.
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PDB code:
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A.E.Sauer-Eriksson,
and
T.Hainzl
(2003).
S-domain assembly of the signal recognition particle.
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Curr Opin Struct Biol,
13,
64-70.
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J.Deng,
Y.Xiong,
B.Pan,
and
M.Sundaralingam
(2003).
Structure of an RNA dodecamer containing a fragment from SRP domain IV of Escherichia coli.
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Acta Crystallogr D Biol Crystallogr,
59,
1004-1011.
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PDB code:
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K.Nagai,
C.Oubridge,
A.Kuglstatter,
E.Menichelli,
C.Isel,
and
L.Jovine
(2003).
Structure, function and evolution of the signal recognition particle.
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EMBO J,
22,
3479-3485.
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S.Matsumura,
Y.Ikawa,
and
T.Inoue
(2003).
Biochemical characterization of the kink-turn RNA motif.
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Nucleic Acids Res,
31,
5544-5551.
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A.Kuglstatter,
C.Oubridge,
and
K.Nagai
(2002).
Induced structural changes of 7SL RNA during the assembly of human signal recognition particle.
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Nat Struct Biol,
9,
740-744.
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PDB code:
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C.Oubridge,
A.Kuglstatter,
L.Jovine,
and
K.Nagai
(2002).
Crystal structure of SRP19 in complex with the S domain of SRP RNA and its implication for the assembly of the signal recognition particle.
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Mol Cell,
9,
1251-1261.
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PDB code:
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G.B.Fogel,
V.W.Porto,
D.G.Weekes,
D.B.Fogel,
R.H.Griffey,
J.A.McNeil,
E.Lesnik,
D.J.Ecker,
and
R.Sampath
(2002).
Discovery of RNA structural elements using evolutionary computation.
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Nucleic Acids Res,
30,
5310-5317.
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J.R.Jagath,
N.B.Matassova,
E.de Leeuw,
J.M.Warnecke,
G.Lentzen,
M.V.Rodnina,
J.Luirink,
and
W.Wintermeyer
(2001).
Important role of the tetraloop region of 4.5S RNA in SRP binding to its receptor FtsY.
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RNA,
7,
293-301.
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R.J.Keenan,
D.M.Freymann,
R.M.Stroud,
and
P.Walter
(2001).
The signal recognition particle.
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Annu Rev Biochem,
70,
755-775.
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T.J.Macke,
D.J.Ecker,
R.R.Gutell,
D.Gautheret,
D.A.Case,
and
R.Sampath
(2001).
RNAMotif, an RNA secondary structure definition and search algorithm.
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Nucleic Acids Res,
29,
4724-4735.
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J.L.Diener,
and
C.Wilson
(2000).
Role of SRP19 in assembly of the Archaeoglobus fulgidus signal recognition particle.
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Biochemistry,
39,
12862-12874.
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L.Jovine,
T.Hainz,
C.Oubridge,
and
K.Nagai
(2000).
Crystallization and preliminary X-ray analysis of the conserved domain IV of Escherichia coli 4.5S RNA.
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Acta Crystallogr D Biol Crystallogr,
56,
1033-1037.
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L.Jovine,
T.Hainzl,
C.Oubridge,
W.G.Scott,
J.Li,
T.K.Sixma,
A.Wonacott,
T.Skarzynski,
and
K.Nagai
(2000).
Crystal structure of the ffh and EF-G binding sites in the conserved domain IV of Escherichia coli 4.5S RNA.
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Structure,
8,
527-540.
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PDB code:
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P.B.Rupert,
and
A.R.Ferré-D'amaré
(2000).
SRPrises in RNA-protein recognition.
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Structure,
8,
R99-104.
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R.M.Stroud,
and
P.Walter
(1999).
Signal sequence recognition and protein targeting.
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Curr Opin Struct Biol,
9,
754-759.
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S.J.Schroeder,
M.E.Burkard,
and
D.H.Turner
(1999).
The energetics of small internal loops in RNA.
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Biopolymers,
52,
157-167.
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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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