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PDBsum entry 1hq1
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Signaling protein/RNA
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PDB id
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1hq1
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.3.6.5.4
- signal-recognition-particle GTPase.
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Reaction:
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GTP + H2O = GDP + phosphate + H+
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GTP
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+
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H2O
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=
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GDP
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+
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phosphate
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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J Mol Biol
307:229-246
(2001)
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PubMed id:
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Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle.
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R.T.Batey,
M.B.Sagar,
J.A.Doudna.
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ABSTRACT
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The signal recognition particle (SRP) is a ribonucleoprotein complex responsible
for targeting proteins to the endoplasmic reticulum in eukarya or to the inner
membrane in prokarya. The crystal structure of the universally conserved
RNA-protein core of the Escherichia coli SRP, refined here to 1.5 A resolution,
revealed minor groove recognition of the 4.5 S RNA component by the M domain of
the Ffh protein. Within the RNA, nucleotides comprising two phylogenetically
conserved internal loops create a unique surface for protein recognition. To
determine the energetic importance of conserved nucleotides for SRP assembly, we
measured the affinity of the M domain for a series of RNA mutants. This analysis
reveals how conserved nucleotides within the two internal loop motifs establish
the architecture of the macromolecular interface and position essential
functional groups for direct recognition by the protein.
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Selected figure(s)
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Figure 6.
Figure 6. Summary of the M domain-RNA interactions and
crystal contacts observed. The intermolecular contacts made by
protein and RNA that are boxed in red. Crystal contacts made by
neighboring complexes in the crystal are boxed in light blue,
purple, orange, and green, with each color representing a
physically distinct molecule. The thick broken lines between
Arg398 and A39, C40 and C41 represent stacking interactions and
blue spheres denote water-mediated interactions.
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Figure 7.
Figure 7. Tetraloop-minor groove interaction. (a) Stereo
representation of the GAAA tetraloop of one molecule interacting
with the minor groove of an adjacent RNA. (b) Base triples
formed by this contact, with the final 2F[o] - F[c] electron
density map contoured at 1.6s superimposed. The hydrogen bond
between A54 and U34 is mediated by a solvent molecule.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2001,
307,
229-246)
copyright 2001.
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Figures were
selected
by an automated process.
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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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D.Lambert,
D.Leipply,
R.Shiman,
and
D.E.Draper
(2009).
The influence of monovalent cation size on the stability of RNA tertiary structures.
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J Mol Biol,
390,
791-804.
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I.A.Buskiewicz,
J.Jöckel,
M.V.Rodnina,
and
W.Wintermeyer
(2009).
Conformation of the signal recognition particle in ribosomal targeting complexes.
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RNA,
15,
44-54.
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T.Oyama,
H.Oka,
K.Mayanagi,
T.Shirai,
K.Matoba,
R.Fujikane,
Y.Ishino,
and
K.Morikawa
(2009).
Atomic structures and functional implications of the archaeal RecQ-like helicase Hjm.
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BMC Struct Biol,
9,
2.
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PDB codes:
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I.J.MacRae,
E.Ma,
M.Zhou,
C.V.Robinson,
and
J.A.Doudna
(2008).
In vitro reconstitution of the human RISC-loading complex.
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Proc Natl Acad Sci U S A,
105,
512-517.
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J.M.Peterson,
and
G.J.Phillips
(2008).
Characterization of conserved bases in 4.5S RNA of Escherichia coli by construction of new F' factors.
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J Bacteriol,
190,
7709-7718.
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X.Zhang,
S.Kung,
and
S.O.Shan
(2008).
Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA.
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J Mol Biol,
381,
581-593.
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A.Y.Keel,
R.P.Rambo,
R.T.Batey,
and
J.S.Kieft
(2007).
A general strategy to solve the phase problem in RNA crystallography.
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Structure,
15,
761-772.
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PDB codes:
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F.Y.Siu,
R.J.Spanggord,
and
J.A.Doudna
(2007).
SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting.
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RNA,
13,
240-250.
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J.Gawronski-Salerno,
J.S.Coon,
P.J.Focia,
and
D.M.Freymann
(2007).
X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases.
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Proteins,
66,
984-995.
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PDB code:
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Q.Vicens,
A.R.Gooding,
A.Laederach,
and
T.R.Cech
(2007).
Local RNA structural changes induced by crystallization are revealed by SHAPE.
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RNA,
13,
536-548.
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X.Zhong,
X.Tao,
J.Stombaugh,
N.Leontis,
and
B.Ding
(2007).
Tertiary structure and function of an RNA motif required for plant vascular entry to initiate systemic trafficking.
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EMBO J,
26,
3836-3846.
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G.Fuchs,
A.J.Stein,
C.Fu,
K.M.Reinisch,
and
S.L.Wolin
(2006).
Structural and biochemical basis for misfolded RNA recognition by the Ro autoantigen.
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Nat Struct Mol Biol,
13,
1002-1009.
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PDB code:
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L.Grajcar,
C.El Amri,
M.Ghomi,
S.Fermandjian,
V.Huteau,
R.Mandel,
S.Lecomte,
and
M.H.Baron
(2006).
Assessment of adenyl residue reactivity within model nucleic acids by surface enhanced Raman spectroscopy.
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Biopolymers,
82,
6.
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S.D.Gilbert,
R.K.Montange,
C.D.Stoddard,
and
R.T.Batey
(2006).
Structural studies of the purine and SAM binding riboswitches.
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Cold Spring Harb Symp Quant Biol,
71,
259-268.
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W.J.Melchers,
J.Zoll,
M.Tessari,
D.V.Bakhmutov,
A.P.Gmyl,
V.I.Agol,
and
H.A.Heus
(2006).
A GCUA tetranucleotide loop found in the poliovirus oriL by in vivo SELEX (un)expectedly forms a YNMG-like structure: Extending the YNMG family with GYYA.
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RNA,
12,
1671-1682.
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PDB code:
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A.J.Stein,
G.Fuchs,
C.Fu,
S.L.Wolin,
and
K.M.Reinisch
(2005).
Structural insights into RNA quality control: the Ro autoantigen binds misfolded RNAs via its central cavity.
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Cell,
121,
529-539.
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PDB codes:
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I.Buskiewicz,
A.Kubarenko,
F.Peske,
M.V.Rodnina,
and
W.Wintermeyer
(2005).
Domain rearrangement of SRP protein Ffh upon binding 4.5S RNA and the SRP receptor FtsY.
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RNA,
11,
947-957.
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L.B.Szewczak,
J.S.Gabrielsen,
S.J.Degregorio,
S.A.Strobel,
and
J.A.Steitz
(2005).
Molecular basis for RNA kink-turn recognition by the h15.5K small RNP protein.
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RNA,
11,
1407-1419.
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R.J.Spanggord,
F.Siu,
A.Ke,
and
J.A.Doudna
(2005).
RNA-mediated interaction between the peptide-binding and GTPase domains of the signal recognition particle.
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Nat Struct Mol Biol,
12,
1116-1122.
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S.Q.Gu,
J.Jöckel,
P.Beinker,
J.Warnecke,
Y.P.Semenkov,
M.V.Rodnina,
and
W.Wintermeyer
(2005).
Conformation of 4.5S RNA in the signal recognition particle and on the 30S ribosomal subunit.
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RNA,
11,
1374-1384.
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I.W.Davis,
L.W.Murray,
J.S.Richardson,
and
D.C.Richardson
(2004).
MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes.
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Nucleic Acids Res,
32,
W615-W619.
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J.A.Doudna,
and
R.T.Batey
(2004).
Structural insights into the signal recognition particle.
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Annu Rev Biochem,
73,
539-557.
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M.Marino
(2004).
Biography of Jennifer A. Doudna.
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Proc Natl Acad Sci U S A,
101,
16987-16989.
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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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C.C.Correll,
and
K.Swinger
(2003).
Common and distinctive features of GNRA tetraloops based on a GUAA tetraloop structure at 1.4 A resolution.
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RNA,
9,
355-363.
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PDB code:
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H.Yang,
F.Jossinet,
N.Leontis,
L.Chen,
J.Westbrook,
H.Berman,
and
E.Westhof
(2003).
Tools for the automatic identification and classification of RNA base pairs.
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Nucleic Acids Res,
31,
3450-3460.
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J.C.Cochrane,
R.T.Batey,
and
S.A.Strobel
(2003).
Quantitation of free energy profiles in RNA-ligand interactions by nucleotide analog interference mapping.
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RNA,
9,
1282-1289.
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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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K.R.Rosendal,
K.Wild,
G.Montoya,
and
I.Sinning
(2003).
Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication.
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Proc Natl Acad Sci U S A,
100,
14701-14706.
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PDB codes:
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S.B.Howerton,
A.Nagpal,
and
L.D.Williams
(2003).
Surprising roles of electrostatic interactions in DNA-ligand complexes.
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Biopolymers,
69,
87-99.
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PDB code:
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T.Leeper,
N.Leulliot,
and
G.Varani
(2003).
The solution structure of an essential stem-loop of human telomerase RNA.
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Nucleic Acids Res,
31,
2614-2621.
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PDB code:
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K.Wild,
O.Weichenrieder,
K.Strub,
I.Sinning,
and
S.Cusack
(2002).
Towards the structure of the mammalian signal recognition particle.
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Curr Opin Struct Biol,
12,
72-81.
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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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}
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