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Contents |
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111 a.a.*
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176 a.a.*
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161 a.a.
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157 a.a.
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97 a.a.
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128 a.a.
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136 a.a.
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89 a.a.*
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70 a.a.*
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103 a.a.*
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77 a.a.*
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26 a.a.*
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88 a.a.
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84 a.a.
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50 a.a.
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73 a.a.
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95 a.a.
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* Residue conservation analysis
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* C-alpha coords only
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PDB id:
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| Name: |
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Ribosome
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Title:
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Structure of functionally activated small ribosomal subunit at 3.3 a resolution
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Structure:
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16s ribosomal RNA. Chain: a. 30s ribosomal protein s2. Chain: b. 30s ribosomal protein s3. Chain: c. 30s ribosomal protein s4. Chain: d. 30s ribosomal protein s5.
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Source:
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Thermus thermophilus. Organism_taxid: 274. Organism_taxid: 274
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Biol. unit:
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20mer (from
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Resolution:
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3.30Å
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R-factor:
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0.304
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R-free:
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0.305
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Authors:
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F.Schluenzen,A.Tocilj,R.Zarivach,J.Harms,M.Gluehmann, D.Janell,A.Bashan,H.Bartels,I.Agmon,F.Franceschi,A.Yonath
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Key ref:
|
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F.Schluenzen
et al.
(2000).
Structure of functionally activated small ribosomal subunit at 3.3 angstroms resolution.
Cell,
102,
615-623.
PubMed id:
DOI:
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Date:
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09-Aug-00
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Release date:
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04-Sep-00
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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No UniProt id for this chain
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P80373
(RS4_THET8) -
30S ribosomal protein S4
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Seq: Struc:
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209 a.a.
161 a.a.
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Q5SHQ5
(RS5_THET8) -
30S ribosomal protein S5
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Seq: Struc:
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162 a.a.
157 a.a.
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Q5SLP8
(RS6_THET8) -
30S ribosomal protein S6
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Seq: Struc:
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101 a.a.
97 a.a.
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P17291
(RS7_THET8) -
30S ribosomal protein S7
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Seq: Struc:
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156 a.a.
128 a.a.
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Q5SHQ2
(RS8_THET8) -
30S ribosomal protein S8
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Seq: Struc:
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138 a.a.
136 a.a.
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No UniProt id for this chain
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No UniProt id for this chain
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No UniProt id for this chain
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No UniProt id for this chain
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No UniProt id for this chain
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Q5SJ76
(RS15_THET8) -
30S ribosomal protein S15
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Seq: Struc:
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89 a.a.
88 a.a.*
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No UniProt id for this chain
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Q5SLQ0
(RS18_THET8) -
30S ribosomal protein S18
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Seq: Struc:
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88 a.a.
50 a.a.*
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Gene Ontology (GO) functional annotation
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Cellular component
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intracellular
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4 terms
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Biological process
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translation
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1 term
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Biochemical function
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structural constituent of ribosome
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5 terms
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DOI no:
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Cell
102:615-623
(2000)
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PubMed id:
|
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| |
|
Structure of functionally activated small ribosomal subunit at 3.3 angstroms resolution.
|
|
F.Schluenzen,
A.Tocilj,
R.Zarivach,
J.Harms,
M.Gluehmann,
D.Janell,
A.Bashan,
H.Bartels,
I.Agmon,
F.Franceschi,
A.Yonath.
|
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| |
ABSTRACT
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| |
|
The small ribosomal subunit performs the decoding of genetic information during
translation. The structure of that from Thermus thermophilus shows that the
decoding center, which positions mRNA and three tRNAs, is constructed entirely
of RNA. The entrance to the mRNA channel will encircle the message when a
latch-like contact closes and contributes to processivity and fidelity. Extended
RNA helical elements that run longitudinally through the body transmit
structural changes, correlating events at the particle's far end with the cycle
of mRNA translocation at the decoding region. 96% of the nucleotides were traced
and the main fold of all proteins was determined. The latter are either
peripheral or appear to serve as linkers. Some may assist the directionality of
translocation.
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Selected figure(s)
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Figure 1.
Figure 1. The Small Subunit and Its Electron Density
Map(Left and center) A stereo representation of the full model
described in this paper. RNA is shown in gold, using a ribbon
backbone and simple lines for base pairs. The differently
colored helical segments and loops are the proteins. The
major subdivisions are labeled: H, head; B, body; S, shoulder;
P, platform; N, nose; F, foot.In all figures, the head is at the
top of the drawing and the foot at the bottom.These portions of
Figure 1 Figure 2 Figure 3 were made with Ribbons (
[12]).(Right) Segments showing RNA (top and middle pannels) and
proteins (bottom) of the MIRAS map at 3.3 Å resolution,
with the model superimposed. Made with O ([32]).
|
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Figure 3.
Figure 3. The Presumed mRNA Path(Left) A surface
representation of the subunit, viewed from the side of the 50S
subunit. The latch is circled in cyan and the decoding center in
red. The mRNA would enter the path in the approximate direction
shown by the dark-blue arrow, pass through the aperture defined
by the latch, and along the channel in the near face of the
subunit. The brown curved arrows show the suggested global
cooperative movements of the platform and the head, which
facilitate the mRNA entrance, progression, and exit.(Right)
Enlarged image of the decoding center region, showing the
positions of tRNA anticodon stem loops and mRNA codons, using
the superposition of tRNA and mRNA from the model of Cate et
al., 1999, as described in the text. The uppermost bulge of H44
is shown in olive, two codons of mRNA in blue, and the anticodon
bases of the tRNA molecules in green (A site), magenta (P site)
and gray (E site). The right side of the figure was made with
DINO ([47]). The contour level is 1.1 standard deviations.
|
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| |
The above figures are
reprinted
by permission from Cell Press:
Cell
(2000,
102,
615-623)
copyright 2000.
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| |
Figures were
selected
by the author.
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Literature references that cite this PDB file's key reference
|
|
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| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
F.A.Rey,
and
W.I.Sundquist
(2011).
Macromolecular assemblages.
|
| |
Curr Opin Struct Biol, 21,
221-222.
|
 |
|
|
|
|
 |
J.Zheng,
C.Wei,
L.Zhao,
L.Liu,
W.Leng,
W.Li,
and
Q.Jin
(2011).
Combining blue native polyacrylamide gel electrophoresis with liquid chromatography tandem mass spectrometry as an effective strategy for analyzing potential membrane protein complexes of Mycobacterium bovis bacillus Calmette-Guérin.
|
| |
BMC Genomics, 12,
40.
|
 |
|
|
|
|
 |
K.Fujii,
M.T.Young,
and
K.D.Harris
(2011).
Exploiting powder X-ray diffraction for direct structure determination in structural biology: The P2X4 receptor trafficking motif YEQGL.
|
| |
J Struct Biol, 174,
461-467.
|
 |
|
|
|
|
 |
M.Valle
(2011).
Almost lost in translation. Cryo-EM of a dynamic macromolecular complex: the ribosome.
|
| |
Eur Biophys J, 40,
589-597.
|
 |
|
|
|
|
 |
Q.Xie,
J.Lin,
Y.Qin,
J.Zhou,
and
W.Bu
(2011).
Structural diversity of eukaryotic 18S rRNA and its impact on alignment and phylogenetic reconstruction.
|
| |
Protein Cell, 2,
161-170.
|
 |
|
|
|
|
 |
A.H.Antonioli,
J.C.Cochrane,
S.V.Lipchock,
and
S.A.Strobel
(2010).
Plasticity of the RNA kink turn structural motif.
|
| |
RNA, 16,
762-768.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
A.Ohman,
T.Oman,
and
M.Oliveberg
(2010).
Solution structures and backbone dynamics of the ribosomal protein S6 and its permutant P(54-55).
|
| |
Protein Sci, 19,
183-189.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
B.M.Burmann,
X.Luo,
P.Rösch,
M.C.Wahl,
and
M.E.Gottesman
(2010).
Fine tuning of the E. coli NusB:NusE complex affinity to BoxA RNA is required for processive antitermination.
|
| |
Nucleic Acids Res, 38,
314-326.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
H.Nanamiya,
and
F.Kawamura
(2010).
Towards an elucidation of the roles of the ribosome during different growth phases in Bacillus subtilis.
|
| |
Biosci Biotechnol Biochem, 74,
451-461.
|
 |
|
|
|
|
 |
J.Frank,
and
R.L.Gonzalez
(2010).
Structure and dynamics of a processive Brownian motor: the translating ribosome.
|
| |
Annu Rev Biochem, 79,
381-412.
|
 |
|
|
|
|
 |
J.Frank
(2010).
The Ribosome Comes Alive.
|
| |
Isr J Chem, 50,
95-98.
|
 |
|
|
|
|
 |
J.P.Armache,
A.Jarasch,
A.M.Anger,
E.Villa,
T.Becker,
S.Bhushan,
F.Jossinet,
M.Habeck,
G.Dindar,
S.Franckenberg,
V.Marquez,
T.Mielke,
M.Thomm,
O.Berninghausen,
B.Beatrix,
J.Söding,
E.Westhof,
D.N.Wilson,
and
R.Beckmann
(2010).
Localization of eukaryote-specific ribosomal proteins in a 5.5-Å cryo-EM map of the 80S eukaryotic ribosome.
|
| |
Proc Natl Acad Sci U S A, 107,
19754-19759.
|
 |
|
PDB codes:
|
 |
|
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|
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|
 |
J.P.Armache,
A.Jarasch,
A.M.Anger,
E.Villa,
T.Becker,
S.Bhushan,
F.Jossinet,
M.Habeck,
G.Dindar,
S.Franckenberg,
V.Marquez,
T.Mielke,
M.Thomm,
O.Berninghausen,
B.Beatrix,
J.Söding,
E.Westhof,
D.N.Wilson,
and
R.Beckmann
(2010).
Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution.
|
| |
Proc Natl Acad Sci U S A, 107,
19748-19753.
|
 |
|
PDB codes:
|
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|
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M.Falb,
I.Amata,
F.Gabel,
B.Simon,
and
T.Carlomagno
(2010).
Structure of the K-turn U4 RNA: a combined NMR and SANS study.
|
| |
Nucleic Acids Res, 38,
6274-6285.
|
 |
|
PDB code:
|
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|
|
|
|
|
 |
M.V.Rodnina,
and
W.Wintermeyer
(2010).
The ribosome goes Nobel.
|
| |
Trends Biochem Sci, 35,
1-5.
|
 |
|
|
|
|
 |
M.Wieland,
B.Berschneider,
M.D.Erlacher,
and
J.S.Hartig
(2010).
Aptazyme-mediated regulation of 16S ribosomal RNA.
|
| |
Chem Biol, 17,
236-242.
|
 |
|
|
|
|
 |
P.C.Whitford,
P.Geggier,
R.B.Altman,
S.C.Blanchard,
J.N.Onuchic,
and
K.Y.Sanbonmatsu
(2010).
Accommodation of aminoacyl-tRNA into the ribosome involves reversible excursions along multiple pathways.
|
| |
RNA, 16,
1196-1204.
|
 |
|
|
|
|
 |
Q.Zeidan,
Z.Wang,
A.De Maio,
and
G.W.Hart
(2010).
O-GlcNAc cycling enzymes associate with the translational machinery and modify core ribosomal proteins.
|
| |
Mol Biol Cell, 21,
1922-1936.
|
 |
|
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|
|
 |
R.Psaila,
D.Ponti,
M.Ponzi,
F.Gigliani,
and
P.A.Battaglia
(2010).
A small sequence in domain v of the mitochondrial large ribosomal RNA restores Drosophila melanogaster pole cell determination in uv-irradiated embryos.
|
| |
Cell Mol Biol Lett, 15,
365-376.
|
 |
|
|
|
|
 |
S.Kimura,
and
T.Suzuki
(2010).
Fine-tuning of the ribosomal decoding center by conserved methyl-modifications in the Escherichia coli 16S rRNA.
|
| |
Nucleic Acids Res, 38,
1341-1352.
|
 |
|
|
|
|
 |
Y.Wei,
and
S.Daunert
(2010).
Enabling technologies in discovery: the 2009 Nobel Prize and its implications in antibiotic design.
|
| |
Anal Bioanal Chem, 396,
1623-1626.
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Z.Dauter,
M.Jaskolski,
and
A.Wlodawer
(2010).
Impact of synchrotron radiation on macromolecular crystallography: a personal view.
|
| |
J Synchrotron Radiat, 17,
433-444.
|
 |
|
|
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|
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A.Yonath
(2009).
Large facilities and the evolving ribosome, the cellular machine for genetic-code translation.
|
| |
J R Soc Interface, 6,
S575-S585.
|
 |
|
|
|
|
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R.P.Hickerson,
L.Lancaster,
H.F.Noller,
and
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Fluorescently labeled ribosomes as a tool for analyzing antibiotic binding.
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| |
RNA, 15,
1597-1604.
|
 |
|
|
|
|
 |
C.W.Carter
(2009).
E pluribus tres: the 2009 nobel prize in chemistry.
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| |
Structure, 17,
1558-1561.
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|
|
|
|
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and
S.A.Woodson
(2009).
A minimized rRNA-binding site for ribosomal protein S4 and its implications for 30S assembly.
|
| |
Nucleic Acids Res, 37,
1886-1896.
|
 |
|
|
|
|
 |
D.M.Hamburg,
M.J.Suh,
and
P.A.Limbach
(2009).
Limited proteolysis analysis of the ribosome is affected by subunit association.
|
| |
Biopolymers, 91,
410-422.
|
 |
|
|
|
|
 |
E.Zimmerman,
and
A.Yonath
(2009).
Biological implications of the ribosome's stunning stereochemistry.
|
| |
Chembiochem, 10,
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|
 |
|
|
|
|
 |
G.Y.Soung,
J.L.Miller,
H.Koc,
and
E.C.Koc
(2009).
Comprehensive analysis of phosphorylated proteins of Escherichia coli ribosomes.
|
| |
J Proteome Res, 8,
3390-3402.
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|
|
|
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H.S.Zaher,
and
R.Green
(2009).
Fidelity at the molecular level: lessons from protein synthesis.
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| |
Cell, 136,
746-762.
|
 |
|
|
|
|
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J.R.Williamson,
V.Ramakrishnan,
T.Steitz,
and
A.Yonath
(2009).
The ribosome at atomic resolution.
|
| |
Cell, 139,
1041-1043.
|
 |
|
|
|
|
 |
J.Sethuraman,
A.Majer,
N.C.Friedrich,
D.R.Edgell,
and
G.Hausner
(2009).
Genes within genes: multiple LAGLIDADG homing endonucleases target the ribosomal protein S3 gene encoded within an rnl group I intron of Ophiostoma and related taxa.
|
| |
Mol Biol Evol, 26,
2299-2315.
|
 |
|
|
|
|
 |
P.B.Moore
(2009).
The ribosome returned.
|
| |
J Biol, 8,
8.
|
 |
|
|
|
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P.Babitzke,
C.S.Baker,
and
T.Romeo
(2009).
Regulation of translation initiation by RNA binding proteins.
|
| |
Annu Rev Microbiol, 63,
27-44.
|
 |
|
|
|
|
 |
P.Ramaswamy,
and
S.A.Woodson
(2009).
S16 throws a conformational switch during assembly of 30S 5' domain.
|
| |
Nat Struct Mol Biol, 16,
438-445.
|
 |
|
|
|
|
 |
P.Ramaswamy,
and
S.A.Woodson
(2009).
Global stabilization of rRNA structure by ribosomal proteins S4, S17, and S20.
|
| |
J Mol Biol, 392,
666-677.
|
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|
|
|
|
 |
S.Shoji,
S.E.Walker,
and
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(2009).
Ribosomal translocation: one step closer to the molecular mechanism.
|
| |
ACS Chem Biol, 4,
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|
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|
|
|
|
 |
S.T.Gregory,
and
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(2009).
Genetic and structural analysis of base substitutions in the central pseudoknot of Thermus thermophilus 16S ribosomal RNA.
|
| |
RNA, 15,
215-223.
|
 |
|
|
|
|
 |
T.J.McLellan,
E.S.Marr,
L.M.Wondrack,
T.A.Subashi,
P.A.Aeed,
S.Han,
Z.Xu,
I.K.Wang,
and
B.A.Maguire
(2009).
A systematic study of 50S ribosomal subunit purification enabling robust crystallization.
|
| |
Acta Crystallogr D Biol Crystallogr, 65,
1270-1282.
|
 |
|
|
|
|
 |
T.Y.Wu,
C.C.Hsieh,
J.J.Hong,
C.Y.Chen,
and
Y.S.Tsai
(2009).
IRSS: a web-based tool for automatic layout and analysis of IRES secondary structure prediction and searching system in silico.
|
| |
BMC Bioinformatics, 10,
160.
|
 |
|
|
|
|
 |
W.Huggins,
S.K.Ghosh,
and
P.Wollenzien
(2009).
Hydrogen bonding and packing density are factors most strongly connected to limiting sites of high flexibility in the 16S rRNA in the 30S ribosome.
|
| |
BMC Struct Biol, 9,
49.
|
 |
|
|
|
|
 |
Y.Xie,
A.V.Dix,
and
Y.Tor
(2009).
FRET enabled real time detection of RNA-small molecule binding.
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