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PDBsum entry 1vox
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234 a.a.
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206 a.a.
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208 a.a.
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150 a.a.
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101 a.a.
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155 a.a.
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138 a.a.
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127 a.a.
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98 a.a.
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119 a.a.
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124 a.a.
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125 a.a.
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60 a.a.
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88 a.a.
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83 a.a.
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104 a.a.
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73 a.a.
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80 a.a.
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99 a.a.
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90 a.a.
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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 basis for the control of translation initiation during stress.
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Authors
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A.Vila-Sanjurjo,
B.S.Schuwirth,
C.W.Hau,
J.H.Cate.
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Ref.
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Nat Struct Mol Biol, 2004,
11,
1054-1059.
[DOI no: ]
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PubMed id
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Abstract
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During environmental stress, organisms limit protein synthesis by storing
inactive ribosomes that are rapidly reactivated when conditions improve. Here we
present structural and biochemical data showing that protein Y, an Escherichia
coli stress protein, fills the tRNA- and mRNA-binding channel of the small
ribosomal subunit to stabilize intact ribosomes. Protein Y inhibits translation
initiation during cold shock but not at normal temperatures. Furthermore,
protein Y competes with conserved translation initiation factors that, in
bacteria, are required for ribosomal subunit dissociation. The mechanism used by
protein Y to reduce translation initiation during stress and quickly release
ribosomes for renewed translation initiation may therefore occur widely in
nature.
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Figure 1.
Figure 1. Structural model of protein Y binding to the ribosome
as determined by X-ray crystallography. (a) Location of PY
density in the 70S ribosome. The 30S subunit is gold, the 50S
subunit is light blue, positive difference electron density is
blue, negative density is red, and PY is cyan. Helix 69 of 23S
rRNA is marked with an asterisk. (b) PY density in the 30S
subunit as seen from the perspective of the subunit interface,
indicated by the arrow in a. The density occurs between the
platform (P) and the head (H) of the 30S subunit. The A, P and E
sites, and the body (B) of the small subunit are marked. (c)
Details of the docking of the N-terminal core of PY (PDB entry
1L4S 3) into the difference electron density. The position of
the disordered C-terminal tail is indicated. The view is from
the perspective of the arrow in b.
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Figure 2.
Figure 2. Details of the PY-binding site within the ribosome.
(a) Stereo view of the location of critical 16S rRNA residues
G926, C1400, C1402 and A1493 (green) relative to PY. Helix 69
(H69) of 23S rRNA is blue. Conserved residues within PY are
magenta^3. (b) Overlap of PY with A- and P-site tRNAs. A-, P-
and E-site tRNAs are cyan, green and gray, respectively. The
positions of the 30S and 50S subunits, the path of mRNA, and the
location of the C-terminal tail of PY are indicated. (c) Overlap
of the difference electron density corresponding to PY with mRNA
(red). The positive density, E-, A- and P-site tRNAs are
color-coded as above. The negative density is not shown for
clarity. The 5' and 3' ends of the mRNA are marked.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2004,
11,
1054-1059)
copyright 2004.
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