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PDBsum entry 4byt
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Contents |
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97 a.a.
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81 a.a.
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63 a.a.
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53 a.a.
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60 a.a.
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71 a.a.
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318 a.a.
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159 a.a.
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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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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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185 a.a.
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96 a.a.
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155 a.a.
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124 a.a.
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150 a.a.
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127 a.a.
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124 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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107 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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References listed in PDB file
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Key reference
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Title
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Molecular architecture of a eukaryotic translational initiation complex.
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Authors
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I.S.Fernández,
X.C.Bai,
T.Hussain,
A.C.Kelley,
J.R.Lorsch,
V.Ramakrishnan,
S.H.Scheres.
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Ref.
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Science, 2013,
342,
1240585.
[DOI no: ]
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PubMed id
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Abstract
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The last step in eukaryotic translational initiation involves the joining of the
large and small subunits of the ribosome, with initiator transfer RNA
(Met-tRNA(i)(Met)) positioned over the start codon of messenger RNA in the P
site. This step is catalyzed by initiation factor eIF5B. We used recent advances
in cryo-electron microscopy (cryo-EM) to determine a structure of the eIF5B
initiation complex to 6.6 angstrom resolution from <3% of the population,
comprising just 5143 particles. The structure reveals conformational changes in
eIF5B, initiator tRNA, and the ribosome that provide insights into the role of
eIF5B in translational initiation. The relatively high resolution obtained from
such a small fraction of a heterogeneous sample suggests a general approach for
characterizing the structure of other dynamic or transient biological complexes.
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