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PDBsum entry 2b9m
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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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24 a.a.
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365 a.a.*
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* C-alpha coords only
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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 structures of the ribosome in complex with release factors rf1 and rf2 bound to a cognate stop codon.
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Authors
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S.Petry,
D.E.Brodersen,
F.V.Murphy,
C.M.Dunham,
M.Selmer,
M.J.Tarry,
A.C.Kelley,
V.Ramakrishnan.
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Ref.
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Cell, 2005,
123,
1255-1266.
[DOI no: ]
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PubMed id
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Abstract
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During protein synthesis, translational release factors catalyze the release of
the polypeptide chain when a stop codon on the mRNA reaches the A site of the
ribosome. The detailed mechanism of this process is currently unknown. We
present here the crystal structures of the ribosome from Thermus thermophilus
with RF1 and RF2 bound to their cognate stop codons, at resolutions of 5.9
Angstrom and 6.7 Angstrom, respectively. The structures reveal details of
interactions of the factors with the ribosome and mRNA, including elements
previously implicated in decoding and peptide release. They also shed light on
conformational changes both in the factors and in the ribosome during
termination. Differences seen in the interaction of RF1 and RF2 with the L11
region of the ribosome allow us to rationalize previous biochemical data.
Finally, this work demonstrates the feasibility of crystallizing ribosomes with
bound factors at a defined state along the translational pathway.
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Figure 4.
Figure 4. Interaction of RF1 with the Decoding Center of
the 30S Subunit, with Overview on the Left and Details on the
Right
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Figure 6.
Figure 6. Interaction of RF1 and RF2 with the L11 Region of
the Ribosome
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2005,
123,
1255-1266)
copyright 2005.
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