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PDBsum entry 4yhh
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Contents |
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226 a.a.
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206 a.a.
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208 a.a.
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157 a.a.
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101 a.a.
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155 a.a.
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138 a.a.
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127 a.a.
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99 a.a.
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115 a.a.
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124 a.a.
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119 a.a.
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60 a.a.
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88 a.a.
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85 a.a.
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104 a.a.
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73 a.a.
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83 a.a.
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99 a.a.
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24 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 characterization of an alternative mode of tigecycline binding to the bacterial ribosome.
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Authors
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A.Schedlbauer,
T.Kaminishi,
B.Ochoa-Lizarralde,
N.Dhimole,
S.Zhou,
J.P.López-Alonso,
S.R.Connell,
P.Fucini.
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Ref.
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Antimicrob Agents Chemother, 2015,
59,
2849-2854.
[DOI no: ]
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PubMed id
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Abstract
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Although both tetracycline and tigecycline inhibit protein synthesis by
sterically hindering the binding of tRNA to the ribosomal A site, tigecycline
shows increased efficacy in both in vitro and in vivo activity assays and
escapes the most common resistance mechanisms associated with the tetracycline
class of antibiotics. These differences in activities are attributed to the
tert-butyl-glycylamido side chain found in tigecycline. Our structural analysis
by X-ray crystallography shows that tigecycline binds the bacterial 30S
ribosomal subunit with its tail in an extended conformation and makes extensive
interactions with the 16S rRNA nucleotide C1054. These interactions restrict the
mobility of C1054 and contribute to the antimicrobial activity of tigecycline,
including its resistance to the ribosomal protection proteins.
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