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PDBsum entry 1vsa
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Contents |
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127 a.a.
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272 a.a.
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201 a.a.
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194 a.a.
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180 a.a.
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173 a.a.
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148 a.a.
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138 a.a.
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122 a.a.
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146 a.a.
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137 a.a.
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118 a.a.
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106 a.a.
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137 a.a.
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117 a.a.
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101 a.a.
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109 a.a.
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92 a.a.
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103 a.a.
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185 a.a.
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76 a.a.
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88 a.a.
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62 a.a.
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60 a.a.
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56 a.a.
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48 a.a.
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63 a.a.
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35 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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Crystal structure of a 70s ribosome-Trna complex reveals functional interactions and rearrangements.
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Authors
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A.Korostelev,
S.Trakhanov,
M.Laurberg,
H.F.Noller.
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Ref.
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Cell, 2006,
126,
1065-1077.
[DOI no: ]
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PubMed id
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Abstract
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Our understanding of the mechanism of protein synthesis has undergone rapid
progress in recent years as a result of low-resolution X-ray and cryo-EM
structures of ribosome functional complexes and high-resolution structures of
ribosomal subunits and vacant ribosomes. Here, we present the crystal structure
of the Thermus thermophilus 70S ribosome containing a model mRNA and two tRNAs
at 3.7 A resolution. Many structural details of the interactions between the
ribosome, tRNA, and mRNA in the P and E sites and the ways in which tRNA
structure is distorted by its interactions with the ribosome are seen.
Differences between the conformations of vacant and tRNA-bound 70S ribosomes
suggest an induced fit of the ribosome structure in response to tRNA binding,
including significant changes in the peptidyl-transferase catalytic site.
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Figure 4.
Figure 4. Interactions between the CCA Tail of tRNA and the
50S E Site
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Figure 5.
Figure 5. Distortion of tRNA Structure in the P and E Sites
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2006,
126,
1065-1077)
copyright 2006.
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