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PDBsum entry 3j80
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206 a.a.
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214 a.a.
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217 a.a.
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260 a.a.
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226 a.a.
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184 a.a.
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188 a.a.
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182 a.a.
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155 a.a.
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150 a.a.
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127 a.a.
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87 a.a.
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129 a.a.
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144 a.a.
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97 a.a.
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81 a.a.
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53 a.a.
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223 a.a.
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206 a.a.
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96 a.a.
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122 a.a.
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123 a.a.
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141 a.a.
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120 a.a.
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145 a.a.
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143 a.a.
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106 a.a.
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70 a.a.
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63 a.a.
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53 a.a.
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69 a.a.
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318 a.a.
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25 a.a.
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96 a.a.
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86 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 changes enable start codon recognition by the eukaryotic translation initiation complex.
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Authors
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T.Hussain,
J.L.Llácer,
I.S.Fernández,
A.Munoz,
P.Martin-Marcos,
C.G.Savva,
J.R.Lorsch,
A.G.Hinnebusch,
V.Ramakrishnan.
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Ref.
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Cell, 2014,
159,
597-607.
[DOI no: ]
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PubMed id
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Abstract
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During eukaryotic translation initiation, initiator tRNA does not insert fully
into the P decoding site on the 40S ribosomal subunit. This conformation (POUT)
is compatible with scanning mRNA for the AUG start codon. Base pairing with AUG
is thought to promote isomerization to a more stable conformation (PIN) that
arrests scanning and promotes dissociation of eIF1 from the 40S subunit. Here,
we present a cryoEM reconstruction of a yeast preinitiation complex at 4.0 Å
resolution with initiator tRNA in the PIN state, prior to eIF1 release. The
structure reveals stabilization of the codon-anticodon duplex by the N-terminal
tail of eIF1A, changes in the structure of eIF1 likely instrumental in its
subsequent release, and changes in the conformation of eIF2. The mRNA traverses
the entire mRNA cleft and makes connections to the regulatory domain of eIF2?,
eIF1A, and ribosomal elements that allow recognition of context nucleotides
surrounding the AUG codon.
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