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PDBsum entry 5mlc
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Contents |
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246 a.a.
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219 a.a.
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205 a.a.
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179 a.a.
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178 a.a.
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45 a.a.
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196 a.a.
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120 a.a.
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182 a.a.
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135 a.a.
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116 a.a.
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118 a.a.
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114 a.a.
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116 a.a.
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134 a.a.
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152 a.a.
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91 a.a.
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129 a.a.
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108 a.a.
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75 a.a.
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94 a.a.
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42 a.a.
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60 a.a.
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61 a.a.
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70 a.a.
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37 a.a.
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107 a.a.
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46 a.a.
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47 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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Cryo-Em structure of the spinach chloroplast ribosome reveals the location of plastid-Specific ribosomal proteins and extensions.
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Authors
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M.Graf,
S.Arenz,
P.Huter,
A.Dönhöfer,
J.Novácek,
D.N.Wilson.
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Ref.
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Nucleic Acids Res, 2017,
45,
2887-2896.
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PubMed id
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Abstract
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Ribosomes are the protein synthesizing machines of the cell. Recent advances in
cryo-EM have led to the determination of structures from a variety of species,
including bacterial 70S and eukaryotic 80S ribosomes as well as mitoribosomes
from eukaryotic mitochondria, however, to date high resolution structures of
plastid 70S ribosomes have been lacking. Here we present a cryo-EM structure of
the spinach chloroplast 70S ribosome, with an average resolution of 5.4 Å for
the small 30S subunit and 3.6 Å for the large 50S ribosomal subunit. The
structure reveals the location of the plastid-specific ribosomal proteins (RPs)
PSRP1, PSRP4, PSRP5 and PSRP6 as well as the numerous plastid-specific
extensions of the RPs. We discover many features by which the plastid-specific
extensions stabilize the ribosome via establishing additional interactions with
surrounding ribosomal RNA and RPs. Moreover, we identify a large conglomerate of
plastid-specific protein mass adjacent to the tunnel exit site that could
facilitate interaction of the chloroplast ribosome with the thylakoid membrane
and the protein-targeting machinery. Comparing the Escherichia coli 70S ribosome
with that of the spinach chloroplast ribosome provides detailed insight into the
co-evolution of RP and rRNA.
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