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PDBsum entry 3jap
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208 a.a.
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222 a.a.
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217 a.a.
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223 a.a.
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260 a.a.
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206 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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96 a.a.
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155 a.a.
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117 a.a.
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150 a.a.
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127 a.a.
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117 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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87 a.a.
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129 a.a.
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144 a.a.
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134 a.a.
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70 a.a.
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98 a.a.
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81 a.a.
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62 a.a.
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53 a.a.
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54 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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111 a.a.
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249 a.a.
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396 a.a.
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128 a.a.
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90 a.a.
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550 a.a.
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634 a.a.
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342 a.a.
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31 a.a.
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52 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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Conformational differences between open and closed states of the eukaryotic translation initiation complex.
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Authors
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J.L.Llácer,
T.Hussain,
L.Marler,
C.E.Aitken,
A.Thakur,
J.R.Lorsch,
A.G.Hinnebusch,
V.Ramakrishnan.
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Ref.
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Mol Cell, 2015,
59,
399-412.
[DOI no: ]
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PubMed id
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Abstract
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Translation initiation in eukaryotes begins with the formation of a
pre-initiation complex (PIC) containing the 40S ribosomal subunit, eIF1, eIF1A,
eIF3, ternary complex (eIF2-GTP-Met-tRNAi), and eIF5. The PIC, in an open
conformation, attaches to the 5' end of the mRNA and scans to locate the start
codon, whereupon it closes to arrest scanning. We present single particle
cryo-electron microscopy (cryo-EM) reconstructions of 48S PICs from yeast in
these open and closed states, at 6.0 Å and 4.9 Å, respectively. These
reconstructions show eIF2β as well as a configuration of eIF3 that appears to
encircle the 40S, occupying part of the subunit interface. Comparison of the
complexes reveals a large conformational change in the 40S head from an open
mRNA latch conformation to a closed one that constricts the mRNA entry channel
and narrows the P site to enclose tRNAi, thus elucidating key events in start
codon recognition.
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