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PDBsum entry 5gad
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Contents |
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271 a.a.
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209 a.a.
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201 a.a.
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177 a.a.
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176 a.a.
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149 a.a.
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125 a.a.
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134 a.a.
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142 a.a.
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123 a.a.
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144 a.a.
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136 a.a.
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125 a.a.
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117 a.a.
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114 a.a.
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117 a.a.
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103 a.a.
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110 a.a.
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95 a.a.
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102 a.a.
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94 a.a.
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76 a.a.
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77 a.a.
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62 a.a.
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58 a.a.
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56 a.a.
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51 a.a.
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46 a.a.
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64 a.a.
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38 a.a.
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450 a.a.
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18 a.a.
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198 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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Structures of the e. Coli translating ribosome with srp and its receptor and with the translocon.
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Authors
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A.Jomaa,
D.Boehringer,
M.Leibundgut,
N.Ban.
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Ref.
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Nat Commun, 2016,
7,
10471.
[DOI no: ]
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PubMed id
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Abstract
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Co-translational protein targeting to membranes is a universally conserved
process. Central steps include cargo recognition by the signal recognition
particle and handover to the Sec translocon. Here we present snapshots of key
co-translational-targeting complexes solved by cryo-electron microscopy at
near-atomic resolution, establishing the molecular contacts between the
Escherichia coli translating ribosome, the signal recognition particle and the
translocon. Our results reveal the conformational changes that regulate the
latching of the signal sequence, the release of the heterodimeric domains of the
signal recognition particle and its receptor, and the handover of the signal
sequence to the translocon. We also observe that the signal recognition particle
and the translocon insert-specific structural elements into the ribosomal tunnel
to remodel it, possibly to sense nascent chains. Our work provides structural
evidence for a conformational state of the signal recognition particle and its
receptor primed for translocon binding to the ribosome-nascent chain complex.
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